› 1q3r

X-ray diffraction
2.9Å resolution

Crystal structure of the chaperonin from Thermococcus strain KS-1 (nucleotide-free form of single mutant)

Released:
DOI: 10.2210/pdb1q3r/pdb
PDB entry 1q3r coloured by chain, front view.
PDB entry 1q3r coloured by chain, side view.
PDB entry 1q3r coloured by chain, top view.
Source organism: Thermococcus sp. JCM 11816
Primary publication:
Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms.
Shomura Y, Yoshida T, Iizuka R, Maruyama T, Yohda M, Miki K
J Mol Biol 335 1265-78 (2004)
PMID: 14729342

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo hexadecamer
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermosome subunit alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 548 amino acids
Theoretical weight: 59.24 KDa
Source organism: Thermococcus sp. JCM 11816
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61112 (Residues: 1-548; Coverage: 100%)
Gene name: thsA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P4212
Unit cell:
a: 210.058Å b: 210.058Å c: 157.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
5 more

7 mentions without citation

Chaperonins: Nanocarriers with Biotechnological Applications.
Pipaón et al. (2021)
6 more