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discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Transporter: maltose ABC transporter

Subunit composition of maltose ABC transporter = [MalK]2[MalF][MalG][MalE]
         maltose ABC transporter - ATP binding subunit = MalK (summary available)
         maltose ABC transporter - membrane subunit = MalF (summary available)
         maltose ABC transporter - membrane subunit = MalG (summary available)
         maltose ABC transporter - periplasmic binding protein = MalE (extended summary available)

Summary:
MalKFGE is a maltose transport system that is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Wu95]. MalE is the periplasmic maltose-binding protein, MalF and MalG are the integral membrane components, and MalK is the ATP-binding component of the ABC transporter, peripherally associated with the inner membrane through its interactions with MalF and MalG. The maltose ABC transporter is capable of transporting malto-oligosaccharides up to seven glucose units long [Ferenci80]. The maltose transporter also functions to regulate gene expression through direct interaction with its cognate transcriptional regulator MalT [Richet12].

The crystal structure of the maltose ABC transporter has been determined in 3 differing conformations: an inward facing 'resting' state with the maltose binding pocket only accessible from the cytoplasm and the nucleotide binding interface in an open conformation [Khare09]; an outward facing conformation with the substrate binding pocket open towards the periplasmic space and ATP bound at the cytoplasmic nucleotide binding interface [Oldham07] and an intermediate 'pre-translocation' structure with an occluded maltose binding pocket and no ATP bound [Oldham11].

The structure of MalE has been studied extensively [Sharff92, Spurlino91, Sharff95, Sharff93, Shilton96a, Quiocho97, Mueller00, Duan01, Duan02, Rubin02, Srinivasan02a, Saul03, Telmer03, Binz04, Telmer05, Kainosho06, Xu06e, Tang07]. The crystal structure of the dimeric MalK has also been determined with bound ADP to a resolution of 2.3 Å [Lu05b], with ATP bound to 2.60 Å, in a nucleotide-free, open state to 2.8 Å, and in a nucleotide-free semi-open state to 2.9 Å [Chen03e]. The N-terminal portion of MalK is the ATP-binding portion which interacts with MalF and MalG, and the C-terminal portion is a regulatory domain that interacts with MalT to prevent transcription of mal genes [Higgins85, Bohm02, Samanta03, Chen03e]. Binding of ATP to MalK is required for stabilization of the MalEFGK2 complex [Chen01f]. Binding of ATP to MalK results in closure of the MalK dimer interface and transmission of a signal through MalF and MalG causing the opening of MalE to release maltose into the transporter [Mourez98, Mannering01, Austermuhle04, Daus06, Oloo06, Wen08]. Binding of MalE to the MalF and MalG subunits of MalFGK2 stimulates ATPase activity of the MalK subunits coupled to substrate transport [Chen01f, Daus07]. The signal for stimulation of ATPase activity is transduced through MalF and MalG [Davidson92, Covitz94]. The interaction of MalF,and in particular the large periplasmic loop of MalF, with MalE has been studied [Daus09, Jacso09].

A 10-fold increase in the level of maltose transport activity was observed in membrane vesicles when the membrane associated components of the transport system (MalF, MalG, and MalK) were overproduced [Davidson90]. Maltose transport activity was abolished in proteoliposomes prepared from a strain with a deletion of the mal genes [Davidson90]. The purified MalKFGE complex exhibits transport-associated ATPase activity, and mutations in the malK gene resulted in loss of ATPase and transport activities without affecting protein stability [Davidson91, Panagiotidis93, Davidson97]. malF mutants are able to transport lactose through the maltose ABC transporter [Merino97, Merino98].

Expression of the malE and malK operons is activated by MalT and cAMP-CRP [VidalIngigliard91, Chapon82, Hofnung74, Hofnung74a]. Inactive (ATP-bound) MalK inhibits the activation of MalT by competing with the binding of the inducer, maltotriose, to MalT [Joly04, Reyes88]. MalK with hydrolysed ATP no longer associates with and inhibits MalT [Panagiotidis98]. Inhibition involves sequestration of MalT by the resting form of the MalFGK transporter, not by free MalK. In the absence of maltose, MalT is sequestered by the maltose transporter via a MalK-MalT interaction; upon addition of maltose to the culture medium, MalT is released from the membrane [Richet12]. This mechanism prevents the induction of malT by endogenously produced maltotriose and directly couples transport with the activation of a transcriptional regulator.

MalY and Aes also inhibit activation of MalT by competing with maltotriose [Reidl91, Schreiber00, Clausen00, Joly02, Schlegel02a]. Lrp activates expression of the malE and malK operons [Tchetina95]. Mlc acts as a repressor of malT expression [Decker98]. Transcription of malE is regulated by the CreBC two-component system [Avison01]. MalK activity is also subject to inducer exclusion, that is, direct allosteric inhibition, by the dephosphorylated form of EIIAGlc. Addition of EIIAGlc inhibits the activity of the maltose transporter reconstituted in proteopliposomes [Dean90, Bao13]. The pH-dependent transcription of the maltose regulon is dependent upon the level of cAMP-CRP [Chagneau01, Alonzo98].

Targeting of MalE to the Sec-translocase for transport across the inner membrane is SecB-dependent [Bechtluft07, Baars06]. Insertion of MalF into the cytoplasmic membrane is SecE- and SecA-dependent [Traxler96, Saaf95], though evidence to the contrary has been presented [McGovern91].

Reviews: [Schlegel02, Boos98, Nikaido94, Shuman93, Bordignon10, Gorke12, Chen13c].

Citations: [Daus07a, Sharma05, Richet05, Kennedy04, Steinke01, Sharma00b, Hunke00, ReichSlotky00, Decker99, Kennedy99a, Nelson98, Panagiotidis98a, Hall98, Mourez97, Mourez97a, Dassa97, Lippincott97, Meyer97, Richet96, Zhang96d, Ehrle96, Schneider95, Hekstra93, Boyd93, Dassa93, Dassa93a, Traxler92, Dean92, McGovern91a, Ehrmann91, Ehrmann90, Wyka90, Francoz88, Froshauer88, Newbury87, Boyd87, Ehrmann87, Duplay87, Bukau86, Froshauer84, Kiino84, Bedouelle83, Ohsumi83, Gilson82, Bedouelle82, Ohki82, Shuman82, Bedouelle82a, Shuman81, Colonna81, Wandersman79, Raibaud79, Silhavy79, Raibaud79a, Randall78, Bao13a]

Locations: inner membrane

Relationship Links: PDB:Structure:2R6G , PDB:Structure:3FH6 , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0015768 - maltose transport Inferred from experiment [Davidson91]
Molecular Function: GO:0015423 - maltose-transporting ATPase activity Inferred from experiment [Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment [Ferenci80]
GO:0033613 - activating transcription factor binding Inferred from experiment [Richet12]
Cellular Component: GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson91]


Enzymatic reaction of: maltotetraose ABC transporter (maltose ABC transporter)

EC Number: 3.6.3.-


Enzymatic reaction of: maltotriose ABC transporter (maltose ABC transporter)

EC Number: 3.6.3.-


Enzymatic reaction of: maltose ABC transporter

Synonyms: Transport of maltose

EC Number: 3.6.3.19

Alternative Products for maltose: maltohexaose [Ferenci80 ] , maltopentaose [Ferenci80 ] , maltoheptaose [Ferenci80 ]


Subunit of maltose ABC transporter: maltose ABC transporter - ATP binding subunit

Synonyms: MalB

Gene: malK Accession Numbers: EG10558 (EcoCyc), b4035, ECK4027

Locations: inner membrane

Sequence Length: 371 AAs

Molecular Weight: 40.99 kD (from nucleotide sequence)

Molecular Weight: 43.0 kD (experimental) [Bavoil80]

GO Terms:

Biological Process: GO:0015768 - maltose transport Inferred from experiment Inferred by computational analysis [GOA01a, Davidson91]
GO:0042956 - maltodextrin transport Inferred from experiment [Ferenci80]
GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0055085 - transmembrane transport Inferred by computational analysis [GOA01a]
Molecular Function: GO:0015423 - maltose-transporting ATPase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment Inferred by computational analysis [GOA06, Ferenci80]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016820 - hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Inferred by computational analysis [GOA01a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Wagner08]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Davidson91]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Bavoil80]

MultiFun Terms: metabolism carbon utilization carbon compounds
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily ATP binding cytoplasmic component

Unification Links: DIP:DIP-47850N , EcoliWiki:b4035 , Mint:MINT-1223477 , ModBase:P68187 , PR:PRO_000023151 , Pride:P68187 , Protein Model Portal:P68187 , RefSeq:NP_418459 , SMR:P68187 , String:511145.b4035 , UniProt:P68187

Relationship Links: InterPro:IN-FAMILY:IPR003439 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR008995 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR013611 , InterPro:IN-FAMILY:IPR015855 , InterPro:IN-FAMILY:IPR017871 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1q12 , PDB:Structure:1q1b , PDB:Structure:1Q1E , PDB:Structure:2awn , PDB:Structure:2awo , PDB:Structure:2R6G , PDB:Structure:3FH6 , PDB:Structure:3GD7 , PDB:Structure:3PUV , PDB:Structure:3PUW , PDB:Structure:3PUX , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0 , PDB:Structure:3RLF , PDB:Structure:4JBW , Pfam:IN-FAMILY:PF00005 , Pfam:IN-FAMILY:PF08402 , Prosite:IN-FAMILY:PS00211 , Prosite:IN-FAMILY:PS50893 , Prosite:IN-FAMILY:PS51245 , Smart:IN-FAMILY:SM00382

In Reactions of unknown directionality:

Not in pathways:
MalT + MalK = MalT-MalK

Summary:
MalK is the ATP-binding component of the maltose ABC transporter.

The structure of MalK has been determined to 2.6 Å resolution [Chen03e]. The dynamics of MalK have been analysed using normal mode analysis and residues involved in conformational change identified [Lukman09].

Essentiality data for malK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of maltose ABC transporter: maltose ABC transporter - membrane subunit

Gene: malF Accession Numbers: EG10555 (EcoCyc), b4033, ECK4025

Locations: inner membrane

Sequence Length: 514 AAs

Molecular Weight: 57.013 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0015768 - maltose transport Inferred from experiment [Davidson91]
GO:0042956 - maltodextrin transport Inferred from experiment [Ferenci80]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Oldham11, Daus09]
GO:0015423 - maltose-transporting ATPase activity Inferred from experiment [Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment [Ferenci80]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05, Silhavy76]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Wagner08]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson91]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism carbon utilization carbon compounds
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, membrane component

Unification Links: DIP:DIP-10142N , EcoliWiki:b4033 , PR:PRO_000023148 , Protein Model Portal:P02916 , RefSeq:NP_418457 , SMR:P02916 , String:511145.b4033 , UniProt:P02916

Relationship Links: InterPro:IN-FAMILY:IPR000515 , PDB:Structure:2r6g , PDB:Structure:3FH6 , PDB:Structure:3PUV , PDB:Structure:3PUW , PDB:Structure:3PUX , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0 , PDB:Structure:3RLF , PDB:Structure:4JBW , Pfam:IN-FAMILY:PF00528 , Prosite:IN-FAMILY:PS50928

Summary:
MalF is an integral membrane component of the maltose ABC transporter.

Essentiality data for malF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of maltose ABC transporter: maltose ABC transporter - membrane subunit

Gene: malG Accession Numbers: EG10556 (EcoCyc), b4032, ECK4024

Locations: inner membrane

Sequence Length: 296 AAs

Molecular Weight: 32.225 kD (from nucleotide sequence)

Molecular Weight: 22.0 kD (experimental) [Dassa85]

GO Terms:

Biological Process: GO:0015768 - maltose transport Inferred from experiment [Davidson91]
GO:0042956 - maltodextrin transport Inferred from experiment [Ferenci80]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0015423 - maltose-transporting ATPase activity Inferred from experiment [Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment [Ferenci80]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05, Dassa90]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Wagner08]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson91]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism carbon utilization carbon compounds
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, membrane component

Unification Links: DIP:DIP-59709N , EcoliWiki:b4032 , PR:PRO_000023149 , Pride:P68183 , Protein Model Portal:P68183 , RefSeq:NP_418456 , SMR:P68183 , String:511145.b4032 , UniProt:P68183

Relationship Links: InterPro:IN-FAMILY:IPR000515 , PDB:Structure:2r6g , PDB:Structure:3FH6 , PDB:Structure:3PUV , PDB:Structure:3PUW , PDB:Structure:3PUX , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0 , PDB:Structure:3RLF , PDB:Structure:4JBW , Pfam:IN-FAMILY:PF00528 , Prosite:IN-FAMILY:PS50928

Summary:
MalG is an integral membrane component of the maltose ABC transporter.

Essentiality data for malG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of maltose ABC transporter: maltose ABC transporter - periplasmic binding protein

Synonyms: MBP, maltodextrin binding protein, maltose binding protein

Gene: malE Accession Numbers: EG10554 (EcoCyc), b4034, ECK4026

Locations: inner membrane, periplasmic space

Sequence Length: 396 AAs

Molecular Weight: 43.388 kD (from nucleotide sequence)

Molecular Weight: 44.0 kD (experimental) [Kellermann74]

GO Terms:

Biological Process: GO:0006810 - transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Davidson90]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0008643 - carbohydrate transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Davidson90]
GO:0015768 - maltose transport Inferred from experiment Inferred by computational analysis [GOA01a, Ferenci80, Davidson90, Shuman82a, Davidson91]
GO:0034289 - detection of maltose stimulus Inferred from experiment [Hazelbauer75, Zhang92]
GO:0042956 - maltodextrin transport Inferred from experiment [Ferenci80]
GO:0060326 - cell chemotaxis Inferred from experiment [Hazelbauer75, Zhang92]
Molecular Function: GO:0005215 - transporter activity Inferred from experiment Inferred by computational analysis [GOA01a, Davidson90]
GO:0005515 - protein binding Inferred from experiment [Oldham11, Daus09, Sharma08]
GO:1901982 - maltose binding Inferred from experiment [Kellermann74]
GO:0005363 - maltose transmembrane transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [DiazMejia09, Han13, LopezCampistrou05, Kellermann74]
GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Spurlino91]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson90]
GO:0055052 - ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Inferred from experiment [Davidson90]
GO:1990060 - maltose transport complex Inferred from experiment [Davidson90]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, periplasmic binding component

Unification Links: DIP:DIP-31871N , EcoliWiki:b4034 , ModBase:P0AEX9 , PR:PRO_000023147 , Pride:P0AEX9 , Protein Model Portal:P0AEX9 , RefSeq:NP_418458 , SMR:P0AEX9 , String:511145.b4034 , Swiss-Model:P0AEX9 , UniProt:P0AEX9

Relationship Links: InterPro:IN-FAMILY:IPR006059 , InterPro:IN-FAMILY:IPR006060 , InterPro:IN-FAMILY:IPR006061 , PDB:Structure:1A7L , PDB:Structure:1ANF , PDB:Structure:1DMB , PDB:Structure:1ez9 , PDB:Structure:1ezo , PDB:Structure:1ezp , PDB:Structure:1fqa , PDB:Structure:1fqb , PDB:Structure:1fqc , PDB:Structure:1fqd , PDB:Structure:1HSJ , PDB:Structure:1IUD , PDB:Structure:1jvx , PDB:Structure:1JVY , PDB:Structure:1JW4 , PDB:Structure:1JW5 , PDB:Structure:1lax , PDB:Structure:1LLS , PDB:Structure:1MDP , PDB:Structure:1MDQ , PDB:Structure:1MG1 , PDB:Structure:1MH3 , PDB:Structure:1MH4 , PDB:Structure:1MPB , PDB:Structure:1MPC , PDB:Structure:1MPD , PDB:Structure:1n3w , PDB:Structure:1n3x , PDB:Structure:1nl5 , PDB:Structure:1NMU , PDB:Structure:1OMP , PDB:Structure:1peb , PDB:Structure:1R6Z , PDB:Structure:1svx , PDB:Structure:1T0K , PDB:Structure:1Y4C , PDB:Structure:1YTV , PDB:Structure:1ziu , PDB:Structure:1zjl , PDB:Structure:1ZKB , PDB:Structure:1zmg , PDB:Structure:2d21 , PDB:Structure:2h25 , PDB:Structure:2KLF , PDB:Structure:2NVU , PDB:Structure:2OBG , PDB:Structure:2OK2 , PDB:Structure:2r6g , PDB:Structure:2v93 , PDB:Structure:2VGQ , PDB:Structure:2XZ3 , PDB:Structure:2ZXT , PDB:Structure:3A3C , PDB:Structure:3C4M , PDB:Structure:3CSB , PDB:Structure:3CSG , PDB:Structure:3DM0 , PDB:Structure:3EHS , PDB:Structure:3EHT , PDB:Structure:3EHU , PDB:Structure:3F5F , PDB:Structure:3G7V , PDB:Structure:3G7W , PDB:Structure:3H3G , PDB:Structure:3H4Z , PDB:Structure:3HPI , PDB:Structure:3HST , PDB:Structure:3IO4 , PDB:Structure:3IO6 , PDB:Structure:3IOR , PDB:Structure:3IOT , PDB:Structure:3IOU , PDB:Structure:3IOV , PDB:Structure:3IOW , PDB:Structure:3KJT , PDB:Structure:3L2J , PDB:Structure:3LBS , PDB:Structure:3LC8 , PDB:Structure:3MBP , PDB:Structure:3MP1 , PDB:Structure:3MP6 , PDB:Structure:3MP8 , PDB:Structure:3MQ9 , PDB:Structure:3N94 , PDB:Structure:3O3U , PDB:Structure:3OAI , PDB:Structure:3OSQ , PDB:Structure:3OSR , PDB:Structure:3PGF , PDB:Structure:3PUV , PDB:Structure:3PUW , PDB:Structure:3PUX , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0 , PDB:Structure:3PY7 , PDB:Structure:3Q25 , PDB:Structure:3Q26 , PDB:Structure:3Q27 , PDB:Structure:3Q28 , PDB:Structure:3Q29 , PDB:Structure:3RLF , PDB:Structure:3RUM , PDB:Structure:3SER , PDB:Structure:3SES , PDB:Structure:3SET , PDB:Structure:3SEU , PDB:Structure:3SEV , PDB:Structure:3SEW , PDB:Structure:3SEX , PDB:Structure:3SEY , PDB:Structure:3VFJ , PDB:Structure:3W15 , PDB:Structure:3WAI , PDB:Structure:4B3N , PDB:Structure:4DXB , PDB:Structure:4DXC , PDB:Structure:4EDQ , PDB:Structure:4EGC , PDB:Structure:4EXK , PDB:Structure:4FE8 , PDB:Structure:4FEB , PDB:Structure:4FEC , PDB:Structure:4FED , PDB:Structure:4GIZ , PDB:Structure:4GLI , PDB:Structure:4IFP , PDB:Structure:4IKM , PDB:Structure:4IRL , PDB:Structure:4KYC , PDB:Structure:4KYD , PDB:Structure:4KYE , PDB:Structure:4MBP , Pfam:IN-FAMILY:PF01547 , Prints:IN-FAMILY:PR00181 , Prosite:IN-FAMILY:PS01037

Summary:
malE encodes the periplasmic substrate-binding component of the maltose ABC transporter. MalE, or maltodextrin binding protein (MBP) can bind linear maltodextrins from 2 - 7 glucose units in length but cannot bind the glucose monomer. MBP can also bind cyclic maltodextrins [Kellermann74, Miller83c, Spurlino91]. MBP is essential for the transport of maltose although mutants have been isolated which are able to transport maltose independently of MBP [Shuman82a]

MBP consists of two globular domains separated by a deep groove which contains the maltodextrin binding site. MBP adopts two distinct conformations - an open unliganded form in which the two globular domains are far apart and the binding groove is accessible and a closed liganded structure. Bound maltose is almost completely enclosed and is held in place by hydrogen bonds and Van der Waals interactions [Spurlino91, Sharff92].

Maltose bound MBP has a strong stimulatory effect on the ATPase activity of the maltose transporter (MalFGK2) in vitro [Davidson92, Orelle08]. Both liganded and unliganded forms of MBP interact with the membrane components of the maltose transporter in vitro [Merino95, Bohl95] and unliganded MBP is also able to stimulate the ATPase activity of MalFGK2 [Gould09]. The interaction of both liganded and unliganded MalE with MalFGK2 in different nucleotide states (apo, ADP and ATP) has been investigated [Bohm13]. Dissociation of MBP is not a prerequisite for substrate translocation [Bohm13].

MBP is expressed at very high levels in the periplasm of E. coli growing on maltose [Kellermann74, Dietzel78].

In addition to being the periplasmic substrate-binding component of the maltose ABC transporter, MalE with bound substrate is also able to bind to the chemoreceptor Tar to induce chemotaxis toward maltose. MalE mutants have been identified which are chemotaxis negative for maltose [Hazelbauer75, Zhang92, Zhang99c].

Export of proMalE to the periplasm is dependent on the cytoplasmic chaperone SecB and this process has been extensively studied (reviewed by [Bassford90]

Reviews: [Martineau, Shilton08]

Citations: [Caldelari08, Quiocho79, Walters13, Austermuhle04, Ferenci86, Treptow85, Collier89, Weiss90, Collier88, Gannon89, Strobel93, Rosemond94, Hor93, Treptow88, Bucher11, Hall97, Hall97a, Hall97b, Gardina97, Kossmann88]

Essentiality data for malE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

References

Alonzo98: Alonzo S, Heyde M, Laloi P, Portalier R (1998). "Analysis of the effect exerted by extracellular pH on the maltose regulon in Escherichia coli K-12." Microbiology 144 ( Pt 12);3317-25. PMID: 9884223

Austermuhle04: Austermuhle MI, Hall JA, Klug CS, Davidson AL (2004). "Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport." J Biol Chem 279(27);28243-50. PMID: 15117946

Avison01: Avison MB, Horton RE, Walsh TR, Bennett PM (2001). "Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media." J Biol Chem 276(29);26955-61. PMID: 11350954

Baars06: Baars L, Ytterberg AJ, Drew D, Wagner S, Thilo C, van Wijk KJ, de Gier JW (2006). "Defining the role of the Escherichia coli chaperone SecB using comparative proteomics." J Biol Chem 281(15);10024-34. PMID: 16352602

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bao13: Bao H, Duong F (2013). "Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter." J Biol Chem 288(33);23666-74. PMID: 23821551

Bao13a: Bao H, Duong F (2013). "ATP alone triggers the outward facing conformation of the maltose ATP-binding cassette transporter." J Biol Chem 288(5);3439-48. PMID: 23243313

Bassford90: Bassford PJ (1990). "Export of the periplasmic maltose-binding protein of Escherichia coli." J Bioenerg Biomembr 22(3);401-39. PMID: 2202725

Bavoil80: Bavoil P, Hofnung M, Nikaido H (1980). "Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli." J Biol Chem 255(18);8366-9. PMID: 6997295

Bechtluft07: Bechtluft P, van Leeuwen RG, Tyreman M, Tomkiewicz D, Nouwen N, Tepper HL, Driessen AJ, Tans SJ (2007). "Direct observation of chaperone-induced changes in a protein folding pathway." Science 318(5855);1458-61. PMID: 18048690

Bedouelle82: Bedouelle H, Schmeissner U, Hofnung M, Rosenberg M (1982). "Promoters of the malEFG and malK-lamB operons in Escherichia coli K12." J Mol Biol 161(4);519-31. PMID: 6185687

Bedouelle82a: Bedouelle H, Hofnung M (1982). "A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12." Mol Gen Genet 185(1);82-7. PMID: 6283312

Bedouelle83: Bedouelle H (1983). "Mutations in the promoter regions of the malEFG and malK-lamB operons of Escherichia coli K12." J Mol Biol 170(4);861-82. PMID: 6417341

Binz04: Binz HK, Amstutz P, Kohl A, Stumpp MT, Briand C, Forrer P, Grutter MG, Pluckthun A (2004). "High-affinity binders selected from designed ankyrin repeat protein libraries." Nat Biotechnol 22(5);575-82. PMID: 15097997

Bohl95: Bohl E, Shuman HA, Boos W (1995). "Mathematical treatment of the kinetics of binding protein dependent transport systems reveals that both the substrate loaded and unloaded binding proteins interact with the membrane components." J Theor Biol 172(1);83-94. PMID: 7891451

Bohm02: Bohm A, Diez J, Diederichs K, Welte W, Boos W (2002). "Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly." J Biol Chem 277(5);3708-17. PMID: 11709552

Bohm13: Bohm S, Licht A, Wuttge S, Schneider E, Bordignon E (2013). "Conformational plasticity of the type I maltose ABC importer." Proc Natl Acad Sci U S A 110(14);5492-7. PMID: 23509285

Boos98: Boos W, Shuman H (1998). "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation." Microbiol Mol Biol Rev 62(1);204-29. PMID: 9529892

Bordignon10: Bordignon E, Grote M, Schneider E (2010). "The maltose ATP-binding cassette transporter in the 21st century--towards a structural dynamic perspective on its mode of action." Mol Microbiol 77(6);1354-66. PMID: 20659291

Boyd87: Boyd D, Manoil C, Beckwith J (1987). "Determinants of membrane protein topology." Proc Natl Acad Sci U S A 84(23);8525-9. PMID: 3317413

Boyd93: Boyd D, Traxler B, Beckwith J (1993). "Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions." J Bacteriol 175(2);553-6. PMID: 8419303

Bucher11: Bucher D, Grant BJ, Markwick PR, McCammon JA (2011). "Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics." PLoS Comput Biol 7(4);e1002034. PMID: 21533070

Bukau86: Bukau B, Ehrmann M, Boos W (1986). "Osmoregulation of the maltose regulon in Escherichia coli." J Bacteriol 166(3);884-91. PMID: 2423504

Caldelari08: Caldelari I, Palmer T, Sargent F (2008). "Escherichia coli tat mutant strains are able to transport maltose in the absence of an active malE gene." Arch Microbiol 189(6);597-604. PMID: 18385983

Chagneau01: Chagneau C, Heyde M, Alonso S, Portalier R, Laloi P (2001). "External-pH-dependent expression of the maltose regulon and ompF gene in Escherichia coli is affected by the level of glycerol kinase, encoded by glpK." J Bacteriol 183(19);5675-83. PMID: 11544231

Chapon82: Chapon C (1982). "Role of the catabolite activator protein in the maltose regulon of Escherichia coli." J Bacteriol 150(2);722-9. PMID: 7040340

Chen01f: Chen J, Sharma S, Quiocho FA, Davidson AL (2001). "Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport." Proc Natl Acad Sci U S A 98(4);1525-30. PMID: 11171984

Chen03e: Chen J, Lu G, Lin J, Davidson AL, Quiocho FA (2003). "A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle." Mol Cell 12(3);651-61. PMID: 14527411

Chen13c: Chen J (2013). "Molecular mechanism of the Escherichia coli maltose transporter." Curr Opin Struct Biol. PMID: 23628288

Clausen00: Clausen T, Schlegel A, Peist R, Schneider E, Steegborn C, Chang YS, Haase A, Bourenkov GP, Bartunik HD, Boos W (2000). "X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression." EMBO J 19(5);831-42. PMID: 10698925

Collier88: Collier DN, Bankaitis VA, Weiss JB, Bassford PJ (1988). "The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein." Cell 53(2);273-83. PMID: 2834066

Collier89: Collier DN, Bassford PJ (1989). "Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli." J Bacteriol 171(9);4640-7. PMID: 2670890

Colonna81: Colonna B, Hofnung M (1981). "rho Mutations restore lamB expression in E. coli K12 strains with an inactive malB region." Mol Gen Genet 184(3);479-83. PMID: 6278260

Covitz94: Covitz KM, Panagiotidis CH, Hor LI, Reyes M, Treptow NA, Shuman HA (1994). "Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter." EMBO J 13(7);1752-9. PMID: 8157012

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

Dassa85: Dassa E, Hofnung M (1985). "Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems." EMBO J 4(9);2287-93. PMID: 3000770

Dassa90: Dassa E (1990). "Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12." Mol Gen Genet 222(1);33-6. PMID: 2233678

Dassa93: Dassa E (1993). "Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli." Mol Microbiol 7(1);39-47. PMID: 8437519

Dassa93a: Dassa E, Muir S (1993). "Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli." Mol Microbiol 7(1);29-38. PMID: 8437518

Dassa97: Dassa E, Lambert P (1997). "Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein." Res Microbiol 148(5);389-95. PMID: 9765817

Daus06: Daus ML, Landmesser H, Schlosser A, Muller P, Herrmann A, Schneider E (2006). "ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter." J Biol Chem 281(7);3856-65. PMID: 16352608

Daus07: Daus ML, Berendt S, Wuttge S, Schneider E (2007). "Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle." Mol Microbiol 66(5);1107-22. PMID: 17961142

Daus07a: Daus ML, Grote M, Muller P, Doebber M, Herrmann A, Steinhoff HJ, Dassa E, Schneider E (2007). "ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2)." J Biol Chem 282(31);22387-96. PMID: 17545154

Daus09: Daus ML, Grote M, Schneider E (2009). "The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle." J Bacteriol 191(3);754-61. PMID: 19047355

Davidson90: Davidson AL, Nikaido H (1990). "Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli." J Biol Chem 1990;265(8);4254-60. PMID: 2155217

Davidson91: Davidson AL, Nikaido H (1991). "Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli." J Biol Chem 266(14);8946-51. PMID: 2026607

Davidson92: Davidson AL, Shuman HA, Nikaido H (1992). "Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins." Proc Natl Acad Sci U S A 89(6);2360-4. PMID: 1549599

Davidson97: Davidson AL, Sharma S (1997). "Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli." J Bacteriol 179(17);5458-64. PMID: 9287001

Dean90: Dean DA, Reizer J, Nikaido H, Saier MH (1990). "Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes." J Biol Chem 265(34);21005-10. PMID: 2250006

Dean92: Dean DA, Hor LI, Shuman HA, Nikaido H (1992). "Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli." Mol Microbiol 6(15);2033-40. PMID: 1406246

Decker98: Decker K, Plumbridge J, Boos W (1998). "Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc." Mol Microbiol 1998;27(2);381-90. PMID: 9484893

Decker99: Decker K, Gerhardt F, Boos W (1999). "The role of the trehalose system in regulating the maltose regulon of Escherichia coli." Mol Microbiol 32(4);777-88. PMID: 10361281

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dietzel78: Dietzel I, Kolb V, Boos W (1978). "Pole cap formation in Escherichia coli following induction of the maltose-binding protein." Arch Microbiol 118(2);207-18. PMID: 358938

Duan01: Duan X, Hall JA, Nikaido H, Quiocho FA (2001). "Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding." J Mol Biol 306(5);1115-26. PMID: 11237621

Duan02: Duan X, Quiocho FA (2002). "Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands." Biochemistry 41(3);706-12. PMID: 11790091

Duplay87: Duplay P, Szmelcman S, Bedouelle H, Hofnung M (1987). "Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose." J Mol Biol 194(4);663-73. PMID: 2821264

Ehrle96: Ehrle R, Pick C, Ulrich R, Hofmann E, Ehrmann M (1996). "Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis." J Bacteriol 178(8);2255-62. PMID: 8636026

Ehrmann87: Ehrmann M, Boos W (1987). "Identification of endogenous inducers of the mal regulon in Escherichia coli." J Bacteriol 1987;169(8);3539-45. PMID: 3038842

Ehrmann90: Ehrmann M, Boyd D, Beckwith J (1990). "Genetic analysis of membrane protein topology by a sandwich gene fusion approach." Proc Natl Acad Sci U S A 87(19);7574-8. PMID: 2170984

Ehrmann91: Ehrmann M, Beckwith J (1991). "Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal." J Biol Chem 266(25);16530-3. PMID: 1885584

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Ferenci80: Ferenci T (1980). "The recognition of maltodextrins by Escherichia coli." Eur J Biochem 108(2);631-6. PMID: 6997044

Ferenci86: Ferenci T, Muir M, Lee KS, Maris D (1986). "Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins." Biochim Biophys Acta 860(1);44-50. PMID: 3524683

Francoz88: Francoz E, Dassa E (1988). "3' end of the malEFG operon in E.coli: localization of the transcription termination site." Nucleic Acids Res 1988;16(9);4097-109. PMID: 2836810

Froshauer84: Froshauer S, Beckwith J (1984). "The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region." J Biol Chem 259(17);10896-903. PMID: 6088520

Froshauer88: Froshauer S, Green GN, Boyd D, McGovern K, Beckwith J (1988). "Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli." J Mol Biol 200(3);501-11. PMID: 3294421

Gannon89: Gannon PM, Li P, Kumamoto CA (1989). "The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export." J Bacteriol 171(2);813-8. PMID: 2644237

Gardina97: Gardina PJ, Bormans AF, Hawkins MA, Meeker JW, Manson MD (1997). "Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor." Mol Microbiol 1997;23(6);1181-91. PMID: 9106209

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Gilson82: Gilson E, Nikaido H, Hofnung M (1982). "Sequence of the malK gene in E.coli K12." Nucleic Acids Res 10(22);7449-58. PMID: 6296778

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gorke12: Gorke B (2012). "Killing two birds with one stone: an ABC transporter regulates gene expression through sequestration of a transcriptional regulator at the membrane." Mol Microbiol 85(4);597-601. PMID: 22742494

Gould09: Gould AD, Telmer PG, Shilton BH (2009). "Stimulation of the maltose transporter ATPase by unliganded maltose binding protein." Biochemistry 48(33);8051-61. PMID: 19630440

Hall97: Hall JA, Thorgeirsson TE, Liu J, Shin YK, Nikaido H (1997). "Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling." J Biol Chem 272(28);17610-4. PMID: 9211909

Hall97a: Hall JA, Gehring K, Nikaido H (1997). "Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein." J Biol Chem 272(28);17605-9. PMID: 9211908

Hall97b: Hall JA, Ganesan AK, Chen J, Nikaido H (1997). "Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport." J Biol Chem 272(28);17615-22. PMID: 9211910

Hall98: Hall JA, Davidson AL, Nikaido H (1998). "Preparation and reconstitution of membrane-associated maltose transporter complex of Escherichia coli." Methods Enzymol 292;20-9. PMID: 9711543

Han13: Han MJ, Kim JY, Kim JA (2013). "Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains." J Biosci Bioeng. PMID: 24140104

Hazelbauer75: Hazelbauer GL (1975). "Maltose chemoreceptor of Escherichia coli." J Bacteriol 122(1);206-14. PMID: 1091624

Hekstra93: Hekstra D, Tommassen J (1993). "Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli." J Bacteriol 1993;175(20);6546-52. PMID: 8407831

Higgins85: Higgins CF, Hiles ID, Whalley K, Jamieson DJ (1985). "Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems." EMBO J 4(4);1033-9. PMID: 3926486

Hofnung74: Hofnung M (1974). "Divergent operons and the genetic structure of the maltose B region in Escherichia coli K12." Genetics 76(2);169-84. PMID: 4595640

Hofnung74a: Hofnung M, Hatfield D, Schwartz M (1974). "malB region in Escherichia coli K-12: characterization of new mutations." J Bacteriol 117(1);40-7. PMID: 4587612

Hor93: Hor LI, Shuman HA (1993). "Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex." J Mol Biol 233(4);659-70. PMID: 8411172

Hunke00: Hunke S, Mourez M, Jehanno M, Dassa E, Schneider E (2000). "ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking." J Biol Chem 275(20);15526-34. PMID: 10809785

Jacso09: Jacso T, Grote M, Daus M, Schmieder P, Keller S, Schneider E, Reif B (2009). "The periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE." Biochemistry. PMID: 19159328

Joly02: Joly N, Danot O, Schlegel A, Boos W, Richet E (2002). "The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon." J Biol Chem 277(19);16606-13. PMID: 11867639

Joly04: Joly N, Bohm A, Boos W, Richet E (2004). "MalK, the ATP-binding Cassette Component of the Escherichia coli Maltodextrin Transporter, Inhibits the Transcriptional Activator MalT by Antagonizing Inducer Binding." J Biol Chem 279(32);33123-30. PMID: 15180985

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kainosho06: Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P (2006). "Optimal isotope labelling for NMR protein structure determinations." Nature 440(7080);52-7. PMID: 16511487

Kellermann74: Kellermann O, Szmelcman S (1974). "Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein." Eur J Biochem 47(1);139-49. PMID: 4215651

Kennedy04: Kennedy KA, Gachelet EG, Traxler B (2004). "Evidence for multiple pathways in the assembly of the Escherichia coli maltose transport complex." J Biol Chem 279(32);33290-7. PMID: 15192116

Kennedy99a: Kennedy KA, Traxler B (1999). "MalK forms a dimer independent of its assembly into the MalFGK2 ATP-binding cassette transporter of Escherichia coli." J Biol Chem 274(10);6259-64. PMID: 10037713

Khare09: Khare D, Oldham ML, Orelle C, Davidson AL, Chen J (2009). "Alternating access in maltose transporter mediated by rigid-body rotations." Mol Cell 33(4);528-36. PMID: 19250913

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Kiino84: Kiino DR, Silhavy TJ (1984). "Mutation prlF1 relieves the lethality associated with export of beta-galactosidase hybrid proteins in Escherichia coli." J Bacteriol 158(3);878-83. PMID: 6233268

Kossmann88: Kossmann M, Wolff C, Manson MD (1988). "Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer." J Bacteriol 170(10);4516-21. PMID: 3049536

Lippincott97: Lippincott J, Traxler B (1997). "MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants." J Bacteriol 179(4);1337-43. PMID: 9023220

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lu05b: Lu G, Westbrooks JM, Davidson AL, Chen J (2005). "ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation." Proc Natl Acad Sci U S A 102(50);17969-74. PMID: 16326809

Lukman09: Lukman S, Grant GH (2009). "A network of dynamically conserved residues deciphers the motions of maltose transporter." Proteins 76(3);588-97. PMID: 19274733

Mannering01: Mannering DE, Sharma S, Davidson AL (2001). "Demonstration of conformational changes associated with activation of the maltose transport complex." J Biol Chem 276(15);12362-8. PMID: 11150310

Martineau: Martineau P, Saurin W, Hofnung M, Spurlino JC, Quiocho FA "Progress in the identification of interaction sites on the periplasmic maltose binding protein from E coli." Biochimie 72(6-7);397-402. PMID: 2124143

McGovern91: McGovern K, Beckwith J (1991). "Membrane insertion of the Escherichia coli MalF protein in cells with impaired secretion machinery." J Biol Chem 266(31);20870-6. PMID: 1939136

McGovern91a: McGovern K, Ehrmann M, Beckwith J (1991). "Decoding signals for membrane protein assembly using alkaline phosphatase fusions." EMBO J 10(10);2773-82. PMID: 1915262

Merino95: Merino G, Boos W, Shuman HA, Bohl E (1995). "The inhibition of maltose transport by the unliganded form of the maltose-binding protein of Escherichia coli: experimental findings and mathematical treatment." J Theor Biol 177(2);171-9. PMID: 8558904

Merino97: Merino G, Shuman HA (1997). "Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system." J Bacteriol 179(24);7687-94. PMID: 9401026

Merino98: Merino G, Shuman HA (1998). "Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli." J Biol Chem 273(4);2435-44. PMID: 9442094

Meyer97: Meyer D, Schneider-Fresenius C, Horlacher R, Peist R, Boos W (1997). "Molecular characterization of glucokinase from Escherichia coli K-12." J Bacteriol 179(4);1298-306. PMID: 9023215

Miller83c: Miller DM, Olson JS, Pflugrath JW, Quiocho FA (1983). "Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis." J Biol Chem 258(22);13665-72. PMID: 6358208

Mourez97: Mourez M, Skouloubris S, Betton JM, Dassa E (1997). "Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli." Mol Microbiol 26(4);821-31. PMID: 9427411

Mourez97a: Mourez M, Hofnung M, Dassa E (1997). "Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits." EMBO J 16(11);3066-77. PMID: 9214624

Mourez98: Mourez M, Jehanno M, Schneider E, Dassa E (1998). "In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP." Mol Microbiol 30(2);353-63. PMID: 9791180

Mueller00: Mueller GA, Choy WY, Yang D, Forman-Kay JD, Venters RA, Kay LE (2000). "Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein." J Mol Biol 300(1);197-212. PMID: 10864509

Nelson98: Nelson BD, Traxler B (1998). "Exploring the role of integral membrane proteins in ATP-binding cassette transporters: analysis of a collection of MalG insertion mutants." J Bacteriol 180(9);2507-14. PMID: 9573205

Newbury87: Newbury SF, Smith NH, Higgins CF (1987). "Differential mRNA stability controls relative gene expression within a polycistronic operon." Cell 51(6);1131-43. PMID: 2446776

Nikaido94: Nikaido H (1994). "Maltose transport system of Escherichia coli: an ABC-type transporter." FEBS Lett 346(1);55-8. PMID: 8206159

Ohki82: Ohki M, Ogawa H, Nishimura S (1982). "Synthesis of mRNA of malB operons at specific stages in the cell cycle of Escherichia coli." Ann Microbiol (Paris) 133A(1);71-5. PMID: 7041748

Ohsumi83: Ohsumi M, Sekiya T, Nishimura S, Ohki M (1983). "Nucleotide sequence of the regulatory region of malB operons in E. coli." J Biochem 94(1);243-7. PMID: 6352694

Oldham07: Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J (2007). "Crystal structure of a catalytic intermediate of the maltose transporter." Nature 450(7169);515-21. PMID: 18033289

Oldham11: Oldham ML, Chen J (2011). "Crystal structure of the maltose transporter in a pretranslocation intermediate state." Science 332(6034);1202-5. PMID: 21566157

Oloo06: Oloo EO, Fung EY, Tieleman DP (2006). "The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter." J Biol Chem 281(38);28397-407. PMID: 16877382

Orelle08: Orelle C, Ayvaz T, Everly RM, Klug CS, Davidson AL (2008). "Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter." Proc Natl Acad Sci U S A 105(35);12837-42. PMID: 18725638

Panagiotidis93: Panagiotidis CH, Reyes M, Sievertsen A, Boos W, Shuman HA (1993). "Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter. The maltose transport system of Escherichia coli." J Biol Chem 1993;268(31);23685-96. PMID: 8226895

Panagiotidis98: Panagiotidis CH, Boos W, Shuman HA (1998). "The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon." Mol Microbiol 30(3);535-46. PMID: 9822819

Panagiotidis98a: Panagiotidis CH, Shuman HA (1998). "Maltose transport in Escherichia coli: mutations that uncouple ATP hydrolysis from transport." Methods Enzymol 292;30-9. PMID: 9711544

Quiocho79: Quiocho FA, Meador WE, Pflugrath JW (1979). "Preliminary crystallographic data of receptors for transport and chemotaxis in Escherichia coli: D-galactose and maltose-binding proteins." J Mol Biol 133(1);181-4. PMID: 393831

Quiocho97: Quiocho FA, Spurlino JC, Rodseth LE (1997). "Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor." Structure 5(8);997-1015. PMID: 9309217

Raibaud79: Raibaud O, Clement JM, Hofnung M (1979). "Structure of the malB region in Escherichia coli K12. III. Correlation of the genetic map with the restriction map." Mol Gen Genet 174(3);261-7. PMID: 384168

Raibaud79a: Raibaud O, Roa M, Braun-Breton C, Schwartz M (1979). "Structure of the malB region in Escherichia coli K12. I. Genetic map of the malK-lamB operon." Mol Gen Genet 174(3);241-8. PMID: 384166

Randall78: Randall LL, Hardy SJ, Josefsson LG (1978). "Precursors of three exported proteins in Escherichia coli." Proc Natl Acad Sci U S A 75(3);1209-12. PMID: 349560

ReichSlotky00: Reich-Slotky R, Panagiotidis C, Reyes M, Shuman HA (2000). "The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil." J Bacteriol 182(4);993-1000. PMID: 10648525

Reidl91: Reidl J, Boos W (1991). "The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system." J Bacteriol 173(15);4862-76. PMID: 1856179

Reyes88: Reyes M, Shuman HA (1988). "Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon." J Bacteriol 170(10);4598-602. PMID: 3049541

Richet05: Richet E, Joly N, Danot O (2005). "Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK." J Mol Biol 347(1);1-10. PMID: 15733913

Richet12: Richet E, Davidson AL, Joly N (2012). "The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate." Mol Microbiol 85(4);632-47. PMID: 22715926

Richet96: Richet E (1996). "On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter." J Mol Biol 264(5);852-62. PMID: 9000616

Rosemond94: Rosemond MJ, Strobel SM, Ray PH, Bassford PJ (1994). "Ability of MBP or RBP signal peptides to influence folding and in vitro translocation of wild-type and hybrid precursors." FEBS Lett 349(2);281-5. PMID: 8050582

Rubin02: Rubin SM, Lee SY, Ruiz EJ, Pines A, Wemmer DE (2002). "Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy." J Mol Biol 322(2);425-40. PMID: 12217701

Saaf95: Saaf A, Andersson H, Gafvelin G, von Heijne G (1995). "SecA-dependence of the translocation of a large periplasmic loop in the Escherichia coli MalF inner membrane protein is a function of sequence context." Mol Membr Biol 12(2);209-15. PMID: 7795711

Samanta03: Samanta S, Ayvaz T, Reyes M, Shuman HA, Chen J, Davidson AL (2003). "Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex." J Biol Chem 278(37);35265-71. PMID: 12813052

Saul03: Saul FA, Mourez M, Vulliez-Le Normand B, Sassoon N, Bentley GA, Betton JM (2003). "Crystal structure of a defective folding protein." Protein Sci 12(3);577-85. PMID: 12592028

Schlegel02: Schlegel A, Bohm A, Lee SJ, Peist R, Decker K, Boos W (2002). "Network regulation of the Escherichia coli maltose system." J Mol Microbiol Biotechnol 4(3);301-7. PMID: 11931562

Schlegel02a: Schlegel A, Danot O, Richet E, Ferenci T, Boos W (2002). "The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY." J Bacteriol 184(11);3069-77. PMID: 12003949

Schneider95: Schneider E, Hunke S, Tebbe S (1995). "The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane." J Bacteriol 177(18);5364-7. PMID: 7665528

Schreiber00: Schreiber V, Steegborn C, Clausen T, Boos W, Richet E (2000). "A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors." Mol Microbiol 35(4);765-76. PMID: 10692154

Sharff92: Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA (1992). "Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis." Biochemistry 31(44);10657-63. PMID: 1420181

Sharff93: Sharff AJ, Rodseth LE, Quiocho FA (1993). "Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein." Biochemistry 32(40);10553-9. PMID: 8399200

Sharff95: Sharff AJ, Rodseth LE, Szmelcman S, Hofnung M, Quiocho FA (1995). "Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein." J Mol Biol 246(1);8-13. PMID: 7853407

Sharma00b: Sharma S, Davidson AL (2000). "Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis." J Bacteriol 182(23);6570-6. PMID: 11073897

Sharma05: Sharma S, Davis JA, Ayvaz T, Traxler B, Davidson AL (2005). "Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly." J Bacteriol 187(8);2908-11. PMID: 15805537

Sharma08: Sharma S, Chakraborty K, Muller BK, Astola N, Tang YC, Lamb DC, Hayer-Hartl M, Hartl FU (2008). "Monitoring protein conformation along the pathway of chaperonin-assisted folding." Cell 133(1);142-53. PMID: 18394994

Shilton08: Shilton BH (2008). "The dynamics of the MBP-MalFGK(2) interaction: a prototype for binding protein dependent ABC-transporter systems." Biochim Biophys Acta 1778(9);1772-80. PMID: 17950243

Shilton96a: Shilton BH, Shuman HA, Mowbray SL (1996). "Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein." J Mol Biol 264(2);364-76. PMID: 8951382

Shuman81: Shuman HA, Silhavy TJ (1981). "Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system." J Biol Chem 256(2);560-2. PMID: 6778869

Shuman82: Shuman HA (1982). "The maltose-maltodextrin transport system of Escherichia coli." Ann Microbiol (Paris) 133A(1);153-9. PMID: 7041738

Shuman82a: Shuman HA (1982). "Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane." J Biol Chem 257(10);5455-61. PMID: 7040366

Shuman93: Shuman HA, Panagiotidis CH (1993). "Tinkering with transporters: periplasmic binding protein-dependent maltose transport in E. coli." J Bioenerg Biomembr 25(6);613-20. PMID: 7511584

Silhavy76: Silhavy TJ, Casadaban MJ, Shuman HA, Beckwith JR (1976). "Conversion of beta-galactosidase to a membrane-bound state by gene fusion." Proc Natl Acad Sci U S A 73(10);3423-7. PMID: 790385

Silhavy79: Silhavy TJ, Brickman E, Bassford PJ, Casadaban MJ, Shuman HA, Schwartz V, Guarente L, Schwartz M, Beckwith JR (1979). "Structure of the malB region in Escherichia coli K12. II. Genetic map of the malE,F,G operon." Mol Gen Genet 174(3);249-59. PMID: 384167

Spurlino91: Spurlino JC, Lu GY, Quiocho FA (1991). "The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis." J Biol Chem 266(8);5202-19. PMID: 2002054

Srinivasan02a: Srinivasan U, Iyer GH, Przybycien TA, Samsonoff WA, Bell JA (2002). "Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry." Protein Eng 15(11);895-902. PMID: 12538909

Steinke01: Steinke A, Grau S, Davidson A, Hofmann E, Ehrmann M (2001). "Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis." J Bacteriol 183(1);375-81. PMID: 11114938

Strobel93: Strobel SM, Cannon JG, Bassford PJ (1993). "Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli." J Bacteriol 175(21);6988-95. PMID: 8226642

Tang07: Tang C, Schwieters CD, Clore GM (2007). "Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR." Nature 449(7165);1078-82. PMID: 17960247

Tchetina95: Tchetina E, Newman EB (1995). "Identification of Lrp-regulated genes by inverse PCR and sequencing: regulation of two mal operons of Escherichia coli by leucine-responsive regulatory protein." J Bacteriol 1995;177(10);2679-83. PMID: 7751276

Telmer03: Telmer PG, Shilton BH (2003). "Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants." J Biol Chem 278(36);34555-67. PMID: 12794084

Telmer05: Telmer PG, Shilton BH (2005). "Structural studies of an engineered zinc biosensor reveal an unanticipated mode of zinc binding." J Mol Biol 354(4);829-40. PMID: 16288781

Traxler92: Traxler B, Beckwith J (1992). "Assembly of a hetero-oligomeric membrane protein complex." Proc Natl Acad Sci U S A 89(22);10852-6. PMID: 1438288

Traxler96: Traxler B, Murphy C (1996). "Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery." J Biol Chem 271(21);12394-400. PMID: 8647843

Treptow85: Treptow NA, Shuman HA (1985). "Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system." J Bacteriol 163(2);654-60. PMID: 3894331

Treptow88: Treptow NA, Shuman HA (1988). "Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system." J Mol Biol 202(4);809-22. PMID: 3050132

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

VidalIngigliard91: Vidal-Ingigliardi D, Raibaud O (1991). "Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters." Proc Natl Acad Sci U S A 1991;88(1);229-33. PMID: 1824723

Wagner08: Wagner S, Pop OI, Pop O, Haan GJ, Baars L, Koningstein G, Klepsch MM, Genevaux P, Luirink J, de Gier JW (2008). "Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC." J Biol Chem 283(26);17881-90. PMID: 18456666

Walters13: Walters BT, Mayne L, Hinshaw JR, Sosnick TR, Englander SW (2013). "Folding of a large protein at high structural resolution." Proc Natl Acad Sci U S A 110(47);18898-903. PMID: 24191053

Wandersman79: Wandersman C, Schwartz M, Ferenci T (1979). "Escherichia coli mutants impaired in maltodextrin transport." J Bacteriol 140(1);1-13. PMID: 387714

Weiss90: Weiss JB, Bassford PJ (1990). "The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro." J Bacteriol 172(6);3023-9. PMID: 2188948

Wen08: Wen PC, Tajkhorshid E (2008). "Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis." Biophys J 95(11);5100-10. PMID: 18790847

Wu95: Wu LF, Mandrand-Berthelot MA (1995). "A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions." Biochimie 1995;77(9);744-50. PMID: 8789466

Wyka90: Wyka MA, St John AC (1990). "Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin." Antimicrob Agents Chemother 34(4);534-8. PMID: 2188585

Xu06e: Xu Y, Zheng Y, Fan JS, Yang D (2006). "A new strategy for structure determination of large proteins in solution without deuteration." Nat Methods 3(11);931-7. PMID: 17060917

Zhang92: Zhang Y, Conway C, Rosato M, Suh Y, Manson MD (1992). "Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein." J Biol Chem 267(32);22813-20. PMID: 1429629

Zhang96d: Zhang Y, Mannering DE, Davidson AL, Yao N, Manson MD (1996). "Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis." J Biol Chem 271(30);17881-9. PMID: 8663400

Zhang99c: Zhang Y, Gardina PJ, Kuebler AS, Kang HS, Christopher JA, Manson MD (1999). "Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism." Proc Natl Acad Sci U S A 96(3);939-44. PMID: 9927672


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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