› 2c7e

Electron Microscopy
9.7Å resolution

REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)

Released:
DOI: 10.2210/pdb2c7e/pdb
PDB entry 2c7e coloured by chain, front view.
PDB entry 2c7e coloured by chain, side view.
PDB entry 2c7e coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
ATP-bound states of GroEL captured by cryo-electron microscopy.
Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR
Cell 107 869-79 (2001)
PMID: 11779463
Related structures: EMD-1047

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: 547 amino acids
Theoretical weight: 57.19 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

Ligands and Environments

3 bound ligands:
Ligand K 7 x K
Ligand MG 7 x MG
Ligand ATP 7 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 9.7Å
Relevant EMDB volumes: EMD-1047
Expression system: Escherichia coli

Quick links

Citations

31 review citations

Is allostery an intrinsic property of all dynamic proteins?
Gunasekaran et al. (2004)
30 more

19 mentions without citation

Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.
Thirumalai et al. (2020)
18 more