› 7r9m

Electron Microscopy
4Å resolution

Methanococcus maripaludis chaperonin, closed conformation 2

Released:
DOI: 10.2210/pdb7r9m/pdb
PDB entry 7r9m coloured by chain, front view.
PDB entry 7r9m coloured by chain, side view.
PDB entry 7r9m coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.
Zhao Y, Schmid MF, Frydman J, Chiu W
OpenAccess logo Nat Commun 12 4754 (2021)
PMID: 34362932
Related structures: EMD-24329

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin Chain: J
Molecule details ›
Chain: J
Length: 505 amino acids
Theoretical weight: 54.37 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q877G8 (Residues: 18-522; Coverage: 93%)
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4Å
Relevant EMDB volumes: EMD-24329
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT.
Smith et al. (2022)
2 more