› 3iyf

Electron Microscopy
8Å resolution

Atomic Model of the Lidless Mm-cpn in the Open State

Released:
DOI: 10.2210/pdb3iyf/pdb
PDB entry 3iyf coloured by chain, front view.
PDB entry 3iyf coloured by chain, side view.
PDB entry 3iyf coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Mechanism of folding chamber closure in a group II chaperonin.
Zhang J, Baker ML, Schröder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W
Nature 463 379-83 (2010)
PMID: 20090755
Related structures: EMD-5140

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: 521 amino acids
Theoretical weight: 55.61 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q877G8 (Residues: 1-240, 268-543; 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: 8Å
Relevant EMDB volumes: EMD-5140
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Chaperone machines for protein folding, unfolding and disaggregation.
Saibil H. (2013)
26 more

18 mentions without citation

The Mechanism and Function of Group II Chaperonins.
Lopez et al. (2015)
17 more