› 1g31

X-ray diffraction
2.3Å resolution

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

Released:
DOI: 10.2210/pdb1g31/pdb
PDB entry 1g31 coloured by chain, front view.
PDB entry 1g31 coloured by chain, side view.
PDB entry 1g31 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage.
Hunt JF, van der Vies SM, Henry L, Deisenhofer J
Cell 90 361-71 (1997)
PMID: 9244309

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo heptamer (preferred)
homo tetradecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-148036 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid assembly protein Gp31 Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 111 amino acids
Theoretical weight: 12.09 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P17313 (Residues: 1-111; Coverage: 100%)
Gene name: 31
Sequence domains: Chaperonin 10 Kd subunit
Structure domains: GroES chaperonin

Ligands and Environments

2 bound ligands:
Ligand PO4 19 x PO4
Ligand K 11 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P42212
Unit cell:
a: 157.677Å b: 157.677Å c: 90.932Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.254
Expression system: Escherichia coli

Quick links

Citations

16 review citations

The Hsp70 and Hsp60 chaperone machines.
Bukau et al. (1998)
15 more

6 mentions without citation

Chaperone machines for protein folding, unfolding and disaggregation.
Saibil H. (2013)
5 more