› 1sjp

X-ray diffraction
3.2Å resolution

Mycobacterium tuberculosis Chaperonin60.2

Released:
DOI: 10.2210/pdb1sjp/pdb
PDB entry 1sjp coloured by chain, front view.
PDB entry 1sjp coloured by chain, side view.
PDB entry 1sjp coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis.
Qamra R, Mande SC
J Bacteriol 186 8105-13 (2004)
PMID: 15547284

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161974 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 504 amino acids
Theoretical weight: 53.05 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WPE7 (Residues: 43-540; Coverage: 92%)
Gene names: MTV037.04, Rv0440, cpn60.2, groEL2, groL2, hsp65, mtc28
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 58.674Å b: 113.825Å c: 79.535Å
α: 90° β: 94.585° γ: 90°
R-values:
R R work R free
0.244 0.241 0.285
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Multiple chaperonins in bacteria--why so many?
Lund PA. (2009)
10 more

11 mentions without citation

A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.
Ansari et al. (2018)
10 more