› 4a13

Electron Microscopy
11.3Å resolution

model refined against symmetry-free cryo-EM map of TRiC-ADP

Released:
DOI: 10.2210/pdb4a13/pdb
PDB 4a13 coloured by chain and viewed from the front.
PDB 4a13 coloured by chain and viewed from the side.
PDB 4a13 coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.
Cong Y, Schröder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, Chiu W
OpenAccess logo EMBO J 31 720-30 (2012)
PMID: 22045336
Related structures: EMD-1963

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexadecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T-complex protein 1 subunit beta 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: 55.11 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3ZBH0 (Residues: 14-526; Coverage: 96%)
Gene name: CCT2
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 11.3Å
Relevant EMDB volumes: EMD-1963

Quick links

Citations

8 review citations

Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.
Rodriguez et al. (2020)
7 more

3 mentions without citation

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.
Mattoo et al. (2014)
2 more