› 3rtk

X-ray diffraction
2.8Å resolution

Crystal structure of Cpn60.2 from Mycobacterium tuberculosis at 2.8A

Released:
DOI: 10.2210/pdb3rtk/pdb
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Source organism: Mycobacterium tuberculosis
Primary publication:
The dimeric structure of the Cpn60.2 chaperonin of Mycobacterium tuberculosis at 2.8 Å reveals possible modes of function.
Shahar A, Melamed-Frank M, Kashi Y, Shimon L, Adir N
J Mol Biol 412 192-203 (2011)
PMID: 21802426

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 analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161973 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 546 amino acids
Theoretical weight: 57.62 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPE7 (Residues: 1-540; Coverage: 100%)
Gene names: MTV037.04, Rv0440, cpn60.2, groEL2, groL2, hsp65, mtc28
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 58.19Å b: 111.98Å c: 77.28Å
α: 90° β: 95.5° γ: 90°
R-values:
R R work R free
0.217 0.217 0.285
Expression system: Escherichia coli

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Citations

3 review citations

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.
Henderson et al. (2013)
2 more

10 mentions without citation

A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.
Squeglia et al. (2018)
9 more

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