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PDBsum entry 1jon
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Chaperone PDB id
1jon

 

 

 

 

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Contents
Protein chain
141 a.a. *
Waters ×8
* Residue conservation analysis
PDB id:
1jon
Name: Chaperone
Title: Groel (hsp60 class) fragment comprising residues 191-345
Structure: Groel, hsp60 class. Chain: a. Fragment: polypeptide binding (apical) domain, residues 191 - 345. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: dh5. Organ: tail. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.216     R-free:   0.287
Authors: A.M.Buckle,A.R.Fersht
Key ref: R.Zahn et al. (1996). Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Proc Natl Acad Sci U S A, 93, 15024-15029. PubMed id: 8986757
Date:
30-May-96     Release date:   12-Mar-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0A6F5  (CH60_ECOLI) -  Chaperonin GroEL from Escherichia coli (strain K12)
Seq:
Struc: 		 
Seq:
Struc: 		548 a.a.
141 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.6.1.7  - chaperonin ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
ATP
 + H2O
 + folded polypeptide
 = ADP
 + phosphate
 + unfolded polypeptide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 93:15024-15029 (1996)
PubMed id: 8986757  
 
 
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
R.Zahn, A.M.Buckle, S.Perrett, C.M.Johnson, F.J.Corrales, R.Golbik, A.R.Fersht.
 
  ABSTRACT  
 
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21296677 Y.H.Liu, Y.L.Han, J.Song, Y.Wang, Y.Y.Jing, Q.Shi, C.Tian, Z.Y.Wang, C.P.Li, J.Han, and X.P.Dong (2011).
Heat shock protein 104 inhibited the fibrillization of prion peptide 106-126 and disassembled prion peptide 106-126 fibrils in vitro.
  Int J Biochem Cell Biol, 43, 768-774.  
19564940 V.V.Marchenkov, and G.V.Semisotnov (2009).
GroEL-Assisted Protein Folding: Does It Occur Within the Chaperonin Inner Cavity?
  Int J Mol Sci, 10, 2066-2083.  
18683277 A.Barzegar, A.A.Moosavi-Movahedi, K.Mahnam, H.Bahrami, and N.Sheibani (2008).
Molecular dynamic simulations of nanomechanic chaperone peptide and effects of in silico His mutations on nanostructured function.
  J Pept Sci, 14, 1173-1182.  
17122339 A.Jomaa, D.Damjanovic, V.Leong, R.Ghirlando, J.Iwanczyk, and J.Ortega (2007).
The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.
  J Bacteriol, 189, 706-716.  
16858726 J.P.Lasserre, E.Beyne, S.Pyndiah, D.Lapaillerie, S.Claverol, and M.Bonneu (2006).
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
  Electrophoresis, 27, 3306-3321.  
16614916 L.A.Ramón-Luing, A.Cruz-Migoni, R.Ruíz-Medrano, B.Xoconostle-Cázares, and J.Ortega-Lopez (2006).
One-step purification and immobilization in cellulose of the GroEL apical domain fused to a carbohydrate-binding module and its use in protein refolding.
  Biotechnol Lett, 28, 301-307.  
15331776 A.I.Jewett, A.Baumketner, and J.E.Shea (2004).
Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway.
  Proc Natl Acad Sci U S A, 101, 13192-13197.  
15537752 N.Tanaka, Y.Tani, H.Hattori, T.Tada, and S.Kunugi (2004).
Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity.
  Protein Sci, 13, 3214-3221.  
12923099 P.T.Reddy, C.R.Prasad, P.H.Reddy, D.Reeder, K.McKenney, H.Jaffe, M.N.Dimitrova, A.Ginsburg, A.Peterkofsky, and P.S.Murthy (2003).
Cloning and expression of the gene for a novel protein from Mycobacterium smegmatis with functional similarity to eukaryotic calmodulin.
  J Bacteriol, 185, 5263-5268.  
12012350 D.Gorse (2002).
Application of a chaperone-based refolding method to two- and three-dimensional off-lattice protein models.
  Biopolymers, 64, 146-160.  
12434017 N.Tanaka, S.Nakao, H.Wadai, S.Ikeda, J.Chatellier, and S.Kunugi (2002).
The substrate binding domain of DnaK facilitates slow protein refolding.
  Proc Natl Acad Sci U S A, 99, 15398-15403.  
11598876 D.Gorse (2001).
Global minimization of an off-lattice potential energy function using a chaperone-based refolding method.
  Biopolymers, 59, 411-426.  
11344330 J.D.Fox, R.B.Kapust, and D.S.Waugh (2001).
Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins.
  Protein Sci, 10, 622-630.  
10745098 C.Klanner, W.Neupert, and T.Langer (2000).
The chaperonin-related protein Tcm62p ensures mitochondrial gene expression under heat stress.
  FEBS Lett, 470, 365-369.  
10920207 J.Carmichael, J.Chatellier, A.Woolfson, C.Milstein, A.R.Fersht, and D.C.Rubinsztein (2000).
Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease.
  Proc Natl Acad Sci U S A, 97, 9701-9705.  
10660042 J.L.Feltham, and L.M.Gierasch (2000).
GroEL-substrate interactions: molding the fold, or folding the mold?
  Cell, 100, 193-196.  
10906727 P.A.Voziyan, L.Jadhav, and M.T.Fisher (2000).
Refolding a glutamine synthetase truncation mutant in vitro: identifying superior conditions using a combination of chaperonins and osmolytes.
  J Pharm Sci, 89, 1036-1045.  
10618385 R.Zahn, A.Liu, T.Lührs, R.Riek, C.von Schroetter, F.López García, M.Billeter, L.Calzolai, G.Wider, and K.Wüthrich (2000).
NMR solution structure of the human prion protein.
  Proc Natl Acad Sci U S A, 97, 145-150.
PDB codes: 1qlx 1qlz 1qm0 1qm1 1qm2 1qm3
10384959 M.K.Hayer-Hartl, K.L.Ewalt, and F.U.Hartl (1999).
On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding.
  Biol Chem, 380, 531-540.  
  10548065 Q.Wang, A.M.Buckle, N.W.Foster, C.M.Johnson, and A.R.Fersht (1999).
Design of highly stable functional GroEL minichaperones.
  Protein Sci, 8, 2186-2193.  
10543442 R.Golbik, A.N.Lupas, K.K.Koretke, W.Baumeister, and J.Peters (1999).
The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding.
  Biol Chem, 380, 1049-1062.  
9519301 A.Horovitz (1998).
Structural aspects of GroEL function.
  Curr Opin Struct Biol, 8, 93.  
9860959 A.P.Ben-Zvi, J.Chatellier, A.R.Fersht, and P.Goloubinoff (1998).
Minimal and optimal mechanisms for GroE-mediated protein folding.
  Proc Natl Acad Sci U S A, 95, 15275-15280.  
9584617 A.Richardson, S.J.Landry, and C.Georgopoulos (1998).
The ins and outs of a molecular chaperone machine.
  Trends Biochem Sci, 23, 138-143.  
9808043 F.Weber, F.Keppel, C.Georgopoulos, M.K.Hayer-Hartl, and F.U.Hartl (1998).
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.
  Nat Struct Biol, 5, 977-985.  
9707566 J.Chatellier, F.Hill, P.A.Lund, and A.R.Fersht (1998).
In vivo activities of GroEL minichaperones.
  Proc Natl Acad Sci U S A, 95, 9861-9866.  
9770457 J.D.Wang, M.D.Michelitsch, and J.S.Weissman (1998).
GroEL-GroES-mediated protein folding requires an intact central cavity.
  Proc Natl Acad Sci U S A, 95, 12163-12168.  
9671707 J.Ma, and M.Karplus (1998).
The allosteric mechanism of the chaperonin GroEL: a dynamic analysis.
  Proc Natl Acad Sci U S A, 95, 8502-8507.  
9631288 K.Braig (1998).
Chaperonins.
  Curr Opin Struct Biol, 8, 159-165.  
9812371 L.M.Mutharia, J.Klinck, H.Yamaguchi, and M.Davey (1998).
Purification, characterization and immunochemical properties of a novel 60-kDa protein of Vibrio anguillarum strains.
  FEMS Microbiol Lett, 168, 111-117.  
  9573158 M.Matsuzaki, Y.Kiso, I.Yamamoto, and T.Satoh (1998).
Isolation of a periplasmic molecular chaperone-like protein of Rhodobacter sphaeroides f. sp. denitrificans that is homologous to the dipeptide transport protein DppA of Escherichia coli.
  J Bacteriol, 180, 2718-2722.  
9108017 A.M.Buckle, R.Zahn, and A.R.Fersht (1997).
A structural model for GroEL-polypeptide recognition.
  Proc Natl Acad Sci U S A, 94, 3571-3575.
PDB code: 1kid
8990150 G.M.Clore, and A.M.Gronenborn (1997).
Dissecting intrinsic chaperonin activity.
  Proc Natl Acad Sci U S A, 94, 7-8.  
9302993 H.E.White, S.Chen, A.M.Roseman, O.Yifrach, A.Horovitz, and H.R.Saibil (1997).
Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala.
  Nat Struct Biol, 4, 690-694.  
9276922 J.G.Thomas, A.Ayling, and F.Baneyx (1997).
Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold.
  Appl Biochem Biotechnol, 66, 197-238.  
9108018 M.M.Altamirano, R.Golbik, R.Zahn, A.M.Buckle, and A.R.Fersht (1997).
Refolding chromatography with immobilized mini-chaperones.
  Proc Natl Acad Sci U S A, 94, 3576-3578.  
9303301 O.von Ahsen, M.Tropschug, N.Pfanner, and J.Rassow (1997).
The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form.
  EMBO J, 16, 4568-4578.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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