› 3izm

Electron Microscopy
7.2Å resolution

Mm-cpn wildtype with ATP

Released:
DOI: 10.2210/pdb3izm/pdb
PDB entry 3izm coloured by chain, front view.
PDB entry 3izm coloured by chain, side view.
PDB entry 3izm coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber.
Douglas NR, Reissmann S, Zhang J, Chen B, Jakana J, Kumar R, Chiu W, Frydman J
Cell 144 240-52 (2011)
PMID: 21241893
Related structures: EMD-5249

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
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: 513 amino acids
Theoretical weight: 55.29 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q877G8 (Residues: 7-519; Coverage: 95%)
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 7.2Å
Relevant EMDB volumes: EMD-5249
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Molecular chaperones in protein folding and proteostasis.
Hartl et al. (2011)
15 more