› 1pv2

X-ray diffraction
2.71Å resolution

Native Form 2 E.coli Chaperone Hsp31

Released:
DOI: 10.2210/pdb1pv2/pdb
PDB entry 1pv2 coloured by chain, front view.
PDB entry 1pv2 coloured by chain, side view.
PDB entry 1pv2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.
Quigley PM, Korotkov K, Baneyx F, Hol WG
Protein Sci 13 269-77 (2004)
PMID: 14691241

Function and Biology Details

Reactions catalysed: 
An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate
(R)-lactate = methylglyoxal + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein/nucleic acid deglycase 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 283 amino acids
Theoretical weight: 31.23 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P31658 (Residues: 1-283; Coverage: 100%)
Gene names: JW1950, b1967, hchA, yedU, yzzC
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P1
Unit cell:
a: 54.487Å b: 99.018Å c: 116.795Å
α: 102.95° β: 101.52° γ: 94.19°
R-values:
R R work R free
0.225 0.221 0.286
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Recombinant protein folding and misfolding in Escherichia coli.
Baneyx et al. (2004)
1 more

6 mentions without citation

Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis.
Fong et al. (2009)
5 more