› 3aq1

X-ray diffraction
2.75Å resolution

Open state monomer of a group II chaperonin from methanococcoides burtonii

Released:
DOI: 10.2210/pdb3aq1/pdb
PDB entry 3aq1 coloured by chain, front view.
PDB entry 3aq1 coloured by chain, side view.
PDB entry 3aq1 coloured by chain, top view.
Source organism: Methanococcoides burtonii DSM 6242
Primary publication:
Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer.
Pilak O, Harrop SJ, Siddiqui KS, Chong K, De Francisci D, Burg D, Williams TJ, Cavicchioli R, Curmi PM
Environ Microbiol 13 2232-49 (2011)
PMID: 21477108

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-171495 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermosome subunit Chain: B
Molecule details ›
Chain: B
Length: 500 amino acids
Theoretical weight: 53.93 KDa
Source organism: Methanococcoides burtonii DSM 6242
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12UN6 (Residues: 1-500; Coverage: 100%)
Gene name: Mbur_1960
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: RIGAKU MICROMAX-007 HF
Spacegroup: I222
Unit cell:
a: 63.564Å b: 115.256Å c: 193.864Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.19 0.254
Expression system: Escherichia coli

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Citations

1 review citation

The Mechanism and Function of Group II Chaperonins.
Lopez et al. (2015)
5 other articles