› 4ab2

Electron Microscopy
8.5Å resolution

ATP-triggered molecular mechanics of the chaperonin GroEL

Released:
DOI: 10.2210/pdb4ab2/pdb
PDB entry 4ab2 coloured by chain, front view.
PDB entry 4ab2 coloured by chain, side view.
PDB entry 4ab2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.
Clare DK, Vasishtan D, Stagg S, Quispe J, Farr GW, Topf M, Horwich AL, Saibil HR
OpenAccess logo Cell 149 113-23 (2012)
PMID: 22445172
Related structures: EMD-2002

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 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, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 548 amino acids
Theoretical weight: 57.35 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

Ligands and Environments

3 bound ligands:
Ligand ATP 14 x ATP
Ligand MG 14 x MG
Ligand PO4 14 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 8.5Å
Relevant EMDB volumes: EMD-2002
Expression system: Escherichia coli

Quick links

Citations

31 review citations

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

4 mentions without citation

The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis.
Brandvold et al. (2015)
3 more