spacer
spacer

PDBsum entry 1pv2

Go to PDB code: 
protein Protein-protein interface(s) links
Chaperone PDB id
1pv2
Jmol
Contents
Protein chains
241 a.a. *
257 a.a. *
270 a.a. *
Waters ×72
* Residue conservation analysis
PDB id:
1pv2
Name: Chaperone
Title: Native form 2 e.Coli chaperone hsp31
Structure: Chaperone protein hcha. Chain: a, b, c, d, e, f, g, h. Synonym: hsp31. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: hcha or b1967. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.71Å     R-factor:   0.225     R-free:   0.286
Authors: P.M.Quigley,K.Korotkov,F.Baneyx,W.G.J.Hol
Key ref:
P.M.Quigley et al. (2004). A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function. Protein Sci, 13, 269-277. PubMed id: 14691241 DOI: 10.1110/ps.03399604
Date:
26-Jun-03     Release date:   13-Jan-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P31658  (HCHA_ECOLI) -  Molecular chaperone Hsp31 and glyoxalase 3
Seq:
Struc:
283 a.a.
241 a.a.
Protein chains
Pfam   ArchSchema ?
P31658  (HCHA_ECOLI) -  Molecular chaperone Hsp31 and glyoxalase 3
Seq:
Struc:
283 a.a.
257 a.a.
Protein chains
Pfam   ArchSchema ?
P31658  (HCHA_ECOLI) -  Molecular chaperone Hsp31 and glyoxalase 3
Seq:
Struc:
283 a.a.
270 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H: E.C.4.2.1.130  - D-lactate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (R)-lactate = methylglyoxal + H2O
(R)-lactate
= methylglyoxal
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     response to stress   6 terms 
  Biochemical function     protein binding     7 terms  

 

 
    Added reference    
 
 
DOI no: 10.1110/ps.03399604 Protein Sci 13:269-277 (2004)
PubMed id: 14691241  
 
 
A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.
P.M.Quigley, K.Korotkov, F.Baneyx, W.G.Hol.
 
  ABSTRACT  
 
Heat shock proteins and proteases play a crucial role in cell survival under conditions of environmental stress. The heat shock protein Hsp31, produced by gene hchA at elevated temperatures in Escherichia coli, is a homodimeric protein consisting of a large A domain and a smaller P domain connected by a linker. Two catalytic triads are present per dimer, with the Cys and His contributed by the A domain and an Asp by the P domain. A new crystal Form II confirms the dimer and catalytic triad arrangement seen in the earlier crystal Form I. In addition, several loops exhibit increased flexibility compared to the previous Hsp31 dimer structure. In particular, loops D2 and D3 are intriguing because their mobility leads to the exposure of a sizable hydrophobic patch made up by surface areas of both subunits near the dimer interface. The residues creating this hydrophobic surface are completely conserved in the Hsp31 family. At the same time, access to the catalytic triad is increased. These observations lead to the hypothesis for the functioning of Hsp31 wherein loops D2 and D3 play a key role: first, at elevated temperatures, by becoming mobile and uncovering a large hydrophobic area that helps in binding to client proteins, and second, by removing the client protein from the hydrophobic patch when the temperature decreases and the loops adopt their low-temperature positions at the Hsp31 surface. The proposed mode of action of flexible loops in the functioning of Hsp31 may be a general principle employed by other chaperones.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Comparison of Form I EcHsp31 (top) and Form II EcHsp31 dimer (bottom). Molecular surface of dimers shown with hydrophobic patches in green. Ribbon representation of dimers are shown on the right in the same orientation. Red ribbons in Form I EcHsp31 highlight regions that are disordered in the Form II EcHsp31. Note that the differences (red) between Form I EcHsp31 and Form II EcHsp31 dimer result in the exposure of more hydrophobic regions (green patches) in Form II EcHsp31. These areas are circled in black.
Figure 4.
Figure 4. Molecular surface of Form II EcHsp31 with the linker region from Form I EcHsp31 superimposed to show how Tyr 29 limits access to the active site pocket. The surface of Form II EcHsp31 is colored by domain--A (blue), and P (green), and Cys 185 (yellow). Regions D2 and D3 are modeled in red and orange ball and stick representation from their relative position Form I EcHsp31 structure. Close-up view of the access to Cys 185 of the triad is shown for both Form I and Form II.
 
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2004, 13, 269-277) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19282967 J.H.Fong, B.A.Shoemaker, S.O.Garbuzynskiy, M.Y.Lobanov, O.V.Galzitskaya, and A.R.Panchenko (2009).
Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis.
  PLoS Comput Biol, 5, e1000316.  
19517531 M.S.Sastry, W.Zhou, and F.Baneyx (2009).
Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity.
  Protein Sci, 18, 1439-1447.  
18708355 W.Li, J.Ju, S.R.Rajski, H.Osada, and B.Shen (2008).
Characterization of the tautomycin biosynthetic gene cluster from Streptomyces spiroverticillatus unveiling new insights into dialkylmaleic anhydride and polyketide biosynthesis.
  J Biol Chem, 283, 28607-28617.  
17407165 K.S.Sandhu, and D.Dash (2007).
Dynamic alpha-helices: conformations that do not conform.
  Proteins, 68, 109-122.  
16493650 K.S.Sandhu, and D.Dash (2006).
Conformational flexibility may explain multiple cellular roles of PEST motifs.
  Proteins, 63, 727-732.  
16796689 M.Mujacic, and F.Baneyx (2006).
Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31.
  Mol Microbiol, 60, 1576-1589.  
15529165 F.Baneyx, and M.Mujacic (2004).
Recombinant protein folding and misfolding in Escherichia coli.
  Nat Biotechnol, 22, 1399-1408.  
15173574 M.S.Sastry, P.M.Quigley, W.G.Hol, and F.Baneyx (2004).
The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures.
  Proc Natl Acad Sci U S A, 101, 8587-8592.  
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.