Escherichia coli K-12 substr. MG1655 Enzyme: FKBP-type peptidyl prolyl cis-trans isomerase

Gene: slyD Accession Numbers: EG11663 (EcoCyc), b3349, ECK3336

Synonyms: WHP

Regulation Summary Diagram: ?

Regulation summary diagram for slyD

Subunit composition of FKBP-type peptidyl prolyl cis-trans isomerase = [SlyD]2
         FKBP-type peptidyl prolyl cis-trans isomerase = SlyD

SlyD is a peptidyl prolyl cis/trans-isomerase (PPIase) and chaperone. The protein has a C-terminal metal binding domain and binds Zn2+ and Ni2+ ions [Wulfing94] as well as Cu+ and Co2+ in vitro [Kaluarachchi11]. Its PPIase activity is regulated by Ni2+ binding to the histidine-rich C-terminus [Hottenrott97]. Ni2+ binding increases the thermodynamic stability of both SlyD domains [Haupt11]. In vivo under anaerobic conditions, SlyD can specifically influence the balance of nickel ions in the cell [Kaluarachchi11]. SlyD serves as a Ni2+ reservoir for [NiFe]-hydrogenase biosynthesis [Kaluarachchi11a]. The binding of Cu+ and Ni2+ to two C-terminal peptides has been studied [Witkowska12].

A protein consisting of the N-terminal 165 amino acids of SlyD (SlyD*) efficiently catalyzes refolding of reduced and carboxymethylated RNase T1; the enzyme is inhibited by FK506, and kinetics of the refolding activity have been measured [Scholz06]. The "insert-in-flap" (IF) chaperone domain near the prolyl isomerase active site within SlyD* appears to be necessary and sufficient to confer chaperone activity for proline-limited folding [Knappe07]; it recognizes and binds unfolded and partially folded proteins [Weininger09]. After the IF domain forms an initial dynamic complex with unfolded proteins, they are transferred to the prolyl isomerase domain [Zoldak11]. The substrate specificity of SlyD* was measured using a library of fluorescent peptides, showing high activity with hydrophobic residues such as Leu, Tyr, and Phe preceding proline [Zoldak09]. However, in a protein context, activity was not dependent on the amino acid residue before the proline [Jakob09]. SlyD promotes very fast prolyl isomerization in an unfolded protein; in proteins that already contain the correct prolyl isomer, SlyD thus retards conformational folding [Zoldak13].

SlyD is involved in the insertion of Ni2+ during the maturation of hydrogenases. SlyD has been shown to interact directly with HypB, an accessory protein required for hydrogenase maturation [Zhang05a], and transfers Ni2+ to HypB [Kaluarachchi11a]. A loop in the SlyD chaperone domain is required for interaction with HypB, and the interaction is important for hydrogenase maturation. The C-terminal metal-binding domain of SlyB is required for stimulating metal release from HypB and for hydrogenase activation [Leach07], while the PPIase activity is not required for hydrogenase maturation [Zhang07b]. Interaction with SlyD increases the GTPase activity of HypB [Kaluarachchi11a]. SlyD also interacts directly with HycE, the large subunit of hydrogenase 3, via its IF domain [Chung11]. Although a truncated mutant protein, SlyD155, is able to bind a single Ni2+ ion and interacts with HypB, it is unable to activate release of Ni2+ from HypB and does not activate hydrogenase [Kaluarachchi12].

SlyD (as well as DnaK) binds to Tat signal sequences in vivo and in vitro [Graubner07]. SlyD binds ATP, but does not hydrolyze it; binding is enhanced by bivalent transition metal ions, especially Zn2+ and Ni2+ [Mitterauer99].

SlyD is required for phage φX174-induced cell lysis [Roof94]. Its function appears to be in the stabilization of the φX174 lysis protein E [Bernhardt02]. A peptide consisting of the N-terminal transmembrane domain of protein E inhibits the peptidyl prolyl isomerase activity of SlyD [Mendel06].

Gel filtration experiments indicate that SlyD is a dimer in solution [Mitterauer99], while an N-terminal fragment of SlyD (aa 1-165) appears to be monomeric [Scholz06]. A later study indicates that SlyD is monomeric and contains multiple metal binding sites [Kaluarachchi09]. Solution structures of full-length SlyD [Martino09, Martino09a] and SlyD* [Weininger09] have been solved. The FKBP and IF domains do not have a fixed relative location [Weininger09]. An additional C-terminal α-helix is packed against the atypical PPIase domain and appears to be involved in nickel ion binding and conformational rearrangement of the PPIase domain [Martino09]. The kinetics of folding of the SlyD* protein with or without the IF domain (a "guest domain" located in a loop of the FKBP domain) has been studied [Zoldak09a].

Overexpression of slyD is toxic, causing filamentation [Roof94, Roof97]. In the E. coli B and C strains, slyD mutations cause a significant growth rate defect [Roof97].

SlyD: "sensitivity to lysis D" [Maratea85]

Review: [Kovermann13]

Citations: [Mukherjee03, BolanosGarcia06, Kovermann11, Haupt11a, Kovermann13a]

Locations: cytosol

Map Position: [3,475,929 <- 3,476,519] (74.92 centisomes, 270°)
Length: 591 bp / 196 aa

Molecular Weight of Polypeptide: 20.853 kD (from nucleotide sequence)

Molecular Weight of Multimer: 44 kD (experimental) [Mitterauer99]

Unification Links: ASAP:ABE-0010946 , CGSC:35441 , DIP:DIP-31853N , EchoBASE:EB1614 , EcoGene:EG11663 , EcoliWiki:b3349 , Mint:MINT-1223693 , ModBase:P0A9K9 , OU-Microarray:b3349 , PortEco:slyD , PR:PRO_000023959 , Pride:P0A9K9 , Protein Model Portal:P0A9K9 , RefSeq:NP_417808 , RegulonDB:EG11663 , SMR:P0A9K9 , String:511145.b3349 , UniProt:P0A9K9

Relationship Links: InterPro:IN-FAMILY:IPR001179 , InterPro:IN-FAMILY:IPR023566 , Panther:IN-FAMILY:PTHR10516 , PDB:Structure:2K8I , PDB:Structure:2KFW , Pfam:IN-FAMILY:PF00254 , Prosite:IN-FAMILY:PS50059

In Paralogous Gene Group: 8 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009408 - response to heat Inferred from experiment [Han07]
GO:0022417 - protein maturation by protein folding Inferred from experiment [Zhang05a]
GO:0042026 - protein refolding Inferred from experiment [Scholz06]
GO:0050821 - protein stabilization Inferred from experiment [Han07]
GO:0051604 - protein maturation Inferred from experiment [Leach07]
GO:0000413 - protein peptidyl-prolyl isomerization Inferred by computational analysis [Gaudet10]
GO:0006457 - protein folding Inferred by computational analysis [GOA01]
GO:0061077 - chaperone-mediated protein folding Inferred by computational analysis [Gaudet10]
Molecular Function: GO:0003755 - peptidyl-prolyl cis-trans isomerase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, Zhang07b, Hottenrott97]
GO:0005507 - copper ion binding Inferred from experiment [Kaluarachchi11]
GO:0005515 - protein binding Inferred from experiment [Chan11, Butland05, Chung11, Zhang05a, Butland06]
GO:0008270 - zinc ion binding Inferred from experiment [Kaluarachchi11, Wulfing94]
GO:0016151 - nickel cation binding Inferred from experiment [Kaluarachchi11, Kaluarachchi09, Wulfing94, Martino09]
GO:0050897 - cobalt ion binding Inferred from experiment [Kaluarachchi11]
GO:0051082 - unfolded protein binding Inferred from experiment [Weininger09]
GO:0005528 - FK506 binding Inferred by computational analysis [Gaudet10]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Gaudet10]

MultiFun Terms: information transfer protein related chaperoning, repair (refolding)

Essentiality data for slyD knockouts: ?

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

Created 16-Apr-2007 by Keseler I , SRI International
Last-Curated ? 08-May-2013 by Keseler I , SRI International

Enzymatic reaction of: peptidyl prolyl cis-trans isomerase

Synonyms: peptidylprolyl isomerase, PPIase, rotamase

EC Number:

a [protein]-L-proline (ω = 180) <=> a [protein]-L-proline (ω = 0)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

The apparent Kcat/KM value in a protease-free assay is 2.8x106 M-1s-1 [Zoldak09]. The substrate specificity of the enzyme was measured using a library of fluorescent peptides, showing high activity with hydrophobic residues such as Leu, Tyr, and Phe [Zoldak09].

Kinetic Parameters:

Km (μM)
a [protein]-L-proline (ω = 180)

Sequence Features

Protein sequence of FKBP-type peptidyl prolyl cis-trans isomerase with features indicated

Feature Class Location Citations Comment
Protein-Segment 1 -> 69
UniProt: PPIase first part; Sequence Annotation Type: region of interest;
Conserved-Region 1 -> 95
UniProt: PPIase FKBP-type;
Mutagenesis-Variant 42
[Zhang07b, UniProt15]
UniProt: Decrease in PPIase activity, but has little impact on chaperone activity and interaction with HypB. Almost complete loss of PPIase activity; when associated with Y-132.
Protein-Segment 76 -> 120
UniProt: IF-chaperone; Sequence Annotation Type: region of interest;
Protein-Segment 129 -> 151
UniProt: PPIase second part; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 132
[Zhang07b, UniProt15]
UniProt: Almost complete loss of PPIase activity, but has little impact on chaperone activity and interaction with HypB; when associated with S-42.
Protein-Segment 141 -> 146
UniProt: Glu-rich (acidic); Sequence Annotation Type: compositionally biased region;
Protein-Segment 148 -> 179
UniProt: His-rich (basic); Sequence Annotation Type: compositionally biased region;
Protein-Segment 152 -> 196
UniProt: Metal-binding; Sequence Annotation Type: region of interest;
Protein-Segment 166 -> 194
UniProt: Gly-rich; Sequence Annotation Type: compositionally biased region;
Mutagenesis-Variant 167 -> 168
[Kaluarachchi09, UniProt11]
UniProt: Reduces nickel-binding capacity.
Metal-Binding-Site 167
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 168
UniProt: Nickel; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 184 -> 185
[Kaluarachchi09, UniProt11]
UniProt: Reduces nickel-binding capacity.
Metal-Binding-Site 184
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 185
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 193
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 195
UniProt: Nickel; Non-Experimental Qualifier: potential;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b3349 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11663; confirmed by SwissProt match.


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

Bernhardt02: Bernhardt TG, Roof WD, Young R (2002). "The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174." Mol Microbiol 45(1);99-108. PMID: 12100551

BolanosGarcia06: Bolanos-Garcia VM, Davies OR (2006). "Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography." Biochim Biophys Acta 1760(9);1304-13. PMID: 16814929

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Butland06: Butland G, Zhang JW, Yang W, Sheung A, Wong P, Greenblatt JF, Emili A, Zamble DB (2006). "Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation." FEBS Lett 580(2);677-81. PMID: 16412426

Chan11: Chan Chung KC, Zamble DB (2011). "Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase." J Biol Chem 286(50);43081-90. PMID: 22016389

Chung11: Chung KC, Zamble DB (2011). "The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3." FEBS Lett 585(2);291-4. PMID: 21185288

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Graubner07: Graubner W, Schierhorn A, Bruser T (2007). "DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone." J Biol Chem 282(10);7116-24. PMID: 17215254

Han07: Han KY, Song JA, Ahn KY, Park JS, Seo HS, Lee J (2007). "Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD." Protein Eng Des Sel 20(11);543-9. PMID: 17971396

Haupt11: Haupt C, Weininger U, Kovermann M, Balbach J (2011). "Local and coupled thermodynamic stability of the two-domain and bifunctional enzyme SlyD from Escherichia coli." Biochemistry 50(34);7321-9. PMID: 21770389

Haupt11a: Haupt C, Patzschke R, Weininger U, Groger S, Kovermann M, Balbach J (2011). "Transient enzyme-substrate recognition monitored by real-time NMR." J Am Chem Soc 133(29);11154-62. PMID: 21661729

Hottenrott97: Hottenrott S, Schumann T, Pluckthun A, Fischer G, Rahfeld JU (1997). "The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase." J Biol Chem 272(25);15697-701. PMID: 9188461

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jakob09: Jakob RP, Zoldak G, Aumuller T, Schmid FX (2009). "Chaperone domains convert prolyl isomerases into generic catalysts of protein folding." Proc Natl Acad Sci U S A 106(48);20282-7. PMID: 19920179

Janowski97: Janowski B, Wollner S, Schutkowski M, Fischer G (1997). "A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates." Anal Biochem 252(2);299-307. PMID: 9344417

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

Kaluarachchi09: Kaluarachchi H, Sutherland DE, Young A, Pickering IJ, Stillman MJ, Zamble DB (2009). "The Ni(II)-Binding Properties of the Metallochaperone SlyD." J Am Chem Soc 131(51):18489-500. PMID: 19947632

Kaluarachchi11: Kaluarachchi H, Siebel JF, Kaluarachchi-Duffy S, Krecisz S, Sutherland DE, Stillman MJ, Zamble DB (2011). "Metal selectivity of the Escherichia coli nickel metallochaperone, SlyD." Biochemistry 50(49);10666-77. PMID: 22047179

Kaluarachchi11a: Kaluarachchi H, Zhang JW, Zamble DB (2011). "Escherichia coli SlyD, more than a Ni(II) reservoir." Biochemistry 50(50);10761-3. PMID: 22085337

Kaluarachchi12: Kaluarachchi H, Altenstein M, Sugumar SR, Balbach J, Zamble DB, Haupt C (2012). "Nickel Binding and [NiFe]-Hydrogenase Maturation by the Metallochaperone SlyD with a Single Metal-Binding Site in Escherichia coli." J Mol Biol 417(1-2);28-35. PMID: 22310044

Knappe07: Knappe TA, Eckert B, Schaarschmidt P, Scholz C, Schmid FX (2007). "Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding." J Mol Biol 368(5);1458-68. PMID: 17397867

Kovermann11: Kovermann M, Zierold R, Haupt C, Low C, Balbach J (2011). "NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD." Biochim Biophys Acta 1814(7);873-81. PMID: 21466862

Kovermann13: Kovermann M, Schmid FX, Balbach J (2013). "Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD." Biol Chem 394(8);965-75. PMID: 23585180

Kovermann13a: Kovermann M, Balbach J (2013). "Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein." Biophys Chem 171;16-23. PMID: 23268194

Leach07: Leach MR, Zhang JW, Zamble DB (2007). "The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD." J Biol Chem 282(22);16177-86. PMID: 17426034

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

Maratea85: Maratea D, Young K, Young R (1985). "Deletion and fusion analysis of the phage phi X174 lysis gene E." Gene 40(1);39-46. PMID: 2936651

Martino09: Martino L, He Y, Hands-Taylor KL, Valentine ER, Kelly G, Giancola C, Conte MR (2009). "The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity." FEBS J 276(16);4529-44. PMID: 19645725

Martino09a: Martino L, Kelly G, Conte MR (2009). "Letter to the Editor: resonance assignment of SlyD from E. coli." Biomol NMR Assign 3(2);235-7. PMID: 19760519

Mendel06: Mendel S, Holbourn JM, Schouten JA, Bugg TD (2006). "Interaction of the transmembrane domain of lysis protein E from bacteriophage phiX174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD." Microbiology 152(Pt 10);2959-67. PMID: 17005977

Mitterauer99: Mitterauer T, Nanoff C, Ahorn H, Freissmuth M, Hohenegger M (1999). "Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD." Biochem J 342 ( Pt 1);33-9. PMID: 10432297

Mukherjee03: Mukherjee S, Shukla A, Guptasarma P (2003). "Single-step purification of a protein-folding catalyst, the SlyD peptidyl prolyl isomerase (PPI), from cytoplasmic extracts of Escherichia coli." Biotechnol Appl Biochem 37(Pt 2);183-6. PMID: 12630907

Roof94: Roof WD, Horne SM, Young KD, Young R (1994). "slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases." J Biol Chem 269(4);2902-10. PMID: 8300625

Roof97: Roof WD, Fang HQ, Young KD, Sun J, Young R (1997). "Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family." Mol Microbiol 25(6);1031-46. PMID: 9350861

Scholz06: Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid FX (2006). "SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities." Biochemistry 45(1);20-33. PMID: 16388577

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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

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

Weininger09: Weininger U, Haupt C, Schweimer K, Graubner W, Kovermann M, Bruser T, Scholz C, Schaarschmidt P, Zoldak G, Schmid FX, Balbach J (2009). "NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function." J Mol Biol 387(2);295-305. PMID: 19356587

Witkowska12: Witkowska D, Valensin D, Rowinska-Zyrek M, Karafova A, Kamysz W, Kozlowski H (2012). "Coordination of Ni(2+) and Cu(2+) to metal ion binding domains of E. coli SlyD protein." J Inorg Biochem 107(1);73-81. PMID: 22178668

Wulfing94: Wulfing C, Lombardero J, Pluckthun A (1994). "An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif." J Biol Chem 269(4);2895-901. PMID: 8300624

Zhang05a: Zhang JW, Butland G, Greenblatt JF, Emili A, Zamble DB (2005). "A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway." J Biol Chem 280(6);4360-6. PMID: 15569666

Zhang07b: Zhang JW, Leach MR, Zamble DB (2007). "The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase." J Bacteriol 189(21);7942-4. PMID: 17720786

Zoldak09: Zoldak G, Aumuller T, Lucke C, Hritz J, Oostenbrink C, Fischer G, Schmid FX (2009). "A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases." Biochemistry 48(43);10423-36. PMID: 19785464

Zoldak09a: Zoldak G, Carstensen L, Scholz C, Schmid FX (2009). "Consequences of domain insertion on the stability and folding mechanism of a protein." J Mol Biol 386(4);1138-52. PMID: 19136015

Zoldak11: Zoldak G, Schmid FX (2011). "Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD." J Mol Biol 406(1);176-94. PMID: 21147124

Zoldak13: Zoldak G, Geitner AJ, Schmid FX (2013). "The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client protein." J Am Chem Soc 135(11);4372-9. PMID: 23445547

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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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