› 1mnf

X-ray diffraction
3Å resolution

Domain motions in GroEL upon binding of an oligopeptide

Released:
DOI: 10.2210/pdb1mnf/pdb
PDB entry 1mnf coloured by chain, front view.
PDB entry 1mnf coloured by chain, side view.
PDB entry 1mnf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Domain motions in GroEL upon binding of an oligopeptide.
Wang J, Chen L
J Mol Biol 334 489-99 (2003)
PMID: 14623189

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:
hetero 28-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141320 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: 57.26 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:
12-residue peptide substrate Chains: 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z
Molecule details ›
Chains: 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 12 amino acids
Theoretical weight: 1.46 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 135.415Å b: 260.694Å c: 148.691Å
α: 90° β: 100.94° γ: 90°
R-values:
R R work R free
0.236 0.236 0.259
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

Allosteric regulation of chaperonins.
Horovitz et al. (2005)
5 more

3 mentions without citation

Conformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulations.
Skjaerven et al. (2011)
2 more