› 3j03

Electron Microscopy
4.8Å resolution

Lidless Mm-cpn in the closed state with ATP/AlFx

Released:
DOI: 10.2210/pdb3j03/pdb
PDB entry 3j03 coloured by chain, front view.
PDB entry 3j03 coloured by chain, side view.
PDB entry 3j03 coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.
Zhang J, Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W
Structure 19 633-9 (2011)
PMID: 21565698
Related structures: EMD-5138

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183295 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 491 amino acids
Theoretical weight: 52.62 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q877G8 (Residues: 7-240, 269-519; Coverage: 89%)
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.8Å
Relevant EMDB volumes: EMD-5138
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

6 mentions without citation

Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.
Zhang et al. (2011)
5 more