› 1grl

X-ray diffraction
2.8Å resolution

THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS

Released:
DOI: 10.2210/pdb1grl/pdb
PDB entry 1grl coloured by chain, front view.
PDB entry 1grl coloured by chain, side view.
PDB entry 1grl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB
Nature 371 578-86 (1994)
PMID: 7935790

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

Assemblies composition:
homo tetradecamer
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141322 (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: 548 amino acids
Theoretical weight: 57.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 1-548; 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: 178Å b: 203Å c: 278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.326 0.326 0.368
Expression system: Escherichia coli

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Citations

150 review citations

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

22 mentions without citation

Protein cages, rings and tubes: useful components of future nanodevices?
Heddle JG. (2008)
21 more