› 2eu1

X-ray diffraction
3.29Å resolution

Crystal structure of the chaperonin GroEL-E461K

Released:
DOI: 10.2210/pdb2eu1/pdb
PDB entry 2eu1 coloured by chain, front view.
PDB entry 2eu1 coloured by chain, side view.
PDB entry 2eu1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K.
Cabo-Bilbao A, Spinelli S, Sot B, Agirre J, Mechaly AE, Muga A, Guérin DM
J Struct Biol 155 482-92 (2006)
PMID: 16904907

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

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, 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: 57.39 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
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 267.695Å b: 290.641Å c: 247.006Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.276 0.276 0.296
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structure and allostery of the chaperonin GroEL.
Saibil et al. (2013)
2 more

9 mentions without citation

Rules governing selective protein carbonylation.
Maisonneuve et al. (2009)
8 more