› 1oel

X-ray diffraction
2.8Å resolution

CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1oel/pdb
PDB entry 1oel coloured by chain, front view.
PDB entry 1oel coloured by chain, side view.
PDB entry 1oel coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution.
Braig K, Adams PD, Brünger AT
Nat Struct Biol 2 1083-94 (1995)
PMID: 8846220

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 domains:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 547 amino acids
Theoretical weight: 57.13 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 2-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
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
Spacegroup: C2221
Unit cell:
a: 178.38Å b: 204.98Å c: 280.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.27
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Molecular chaperones in cellular protein folding.
Hartl FU. (1996)
15 more

64 mentions without citation

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