› 3iyg

Electron Microscopy
4Å resolution

Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map

Released:
DOI: 10.2210/pdb3iyg/pdb
PDB entry 3iyg coloured by chain, front view.
PDB entry 3iyg coloured by chain, side view.
PDB entry 3iyg coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Cong Y, Baker ML, Jakana J, Woolford D, Miller EJ, Reissmann S, Kumar RN, Redding-Johanson AM, Batth TS, Mukhopadhyay A, Ludtke SJ, Frydman J, Chiu W
Proc Natl Acad Sci U S A 107 4967-72 (2010)
PMID: 20194787
Related structures: EMD-5148

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-163675 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (8 distinct):
T-complex protein 1 subunit theta Chain: Q
Molecule details ›
Chain: Q
Length: 512 amino acids
Theoretical weight: 55.83 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3ZCI9 (Residues: 17-528; Coverage: 93%)
Gene name: CCT8
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit gamma Chain: G
Molecule details ›
Chain: G
Length: 515 amino acids
Theoretical weight: 57.49 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3T0K2 (Residues: 13-527; Coverage: 95%)
Gene name: CCT3
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit zeta Chain: Z
Molecule details ›
Chain: Z
Length: 517 amino acids
Theoretical weight: 56.6 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q3MHL7 (Residues: 9-344, 345-525; Coverage: 97%)
Gene name: CCT6A
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit delta Chain: D
Molecule details ›
Chain: D
Length: 518 amino acids
Theoretical weight: 56.06 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q2T9X2 (Residues: 25-542; Coverage: 96%)
Gene name: CCT4
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit beta Chain: B
Molecule details ›
Chain: B
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
T-complex protein 1 subunit Chain: E
Molecule details ›
Chain: E
Length: 515 amino acids
Theoretical weight: 56.75 KDa
Source organism: Bos taurus
T-complex protein 1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 529 amino acids
Theoretical weight: 57.5 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q32L40 (Residues: 7-535; Coverage: 95%)
Gene names: CCT1, TCP1
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit eta Chain: H
Molecule details ›
Chain: H
Length: 515 amino acids
Theoretical weight: 56.61 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q2NKZ1 (Residues: 10-524; Coverage: 95%)
Gene name: CCT7
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-5148

Quick links

Citations

20 review citations

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

8 mentions without citation

4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Cong et al. (2010)
7 more