› 1n57

X-ray diffraction
1.6Å resolution

Crystal Structure of Chaperone Hsp31

Released:
DOI: 10.2210/pdb1n57/pdb
PDB entry 1n57 coloured by chain, front view.
PDB entry 1n57 coloured by chain, side view.
PDB entry 1n57 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad.
Quigley PM, Korotkov K, Baneyx F, Hol WG
Proc Natl Acad Sci U S A 100 3137-42 (2003)
PMID: 12621151

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 Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 32.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31658 (Residues: 1-283; Coverage: 100%)
Gene names: JW1950, b1967, hchA, yedU, yzzC
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 52.15Å b: 82Å c: 64.48Å
α: 90° β: 100° γ: 90°
R-values:
R R work R free
0.201 0.187 0.242
Expression system: Escherichia coli BL21(DE3)

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Citations

11 review citations

Molecular pathophysiology of Parkinson's disease.
Moore et al. (2005)
10 more

11 mentions without citation

Bacterial Responses to Glyoxal and Methylglyoxal: Reactive Electrophilic Species.
Lee et al. (2017)
10 more