› 1q3s

X-ray diffraction
3Å resolution

Crystal structure of the chaperonin from Thermococcus strain KS-1 (FormIII crystal complexed with ADP)

Released:
DOI: 10.2210/pdb1q3s/pdb
PDB entry 1q3s coloured by chain, front view.
PDB entry 1q3s coloured by chain, side view.
PDB entry 1q3s 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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158223 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermosome subunit alpha Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 548 amino acids
Theoretical weight: 59.3 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

2 bound ligands:
Ligand MG 7 x MG
Ligand ADP 8 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45PX
Spacegroup: C2221
Unit cell:
a: 207.425Å b: 236.23Å c: 234.106Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.251 0.288
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

10 mentions without citation

Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond.
Sahlan et al. (2018)
9 more