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› 4v94

X-ray diffraction
3.8Å resolution

Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS

Released:
DOI: 10.2210/pdb4v94/pdb
Model geometry
Fit model/data
PDB entry 4v94 coloured by chain, front view.
PDB entry 4v94 coloured by chain, side view.
PDB entry 4v94 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
The molecular architecture of the eukaryotic chaperonin TRiC/CCT.
Leitner A, Joachimiak LA, Bracher A, Mönkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J
Structure 20 814-25 (2012)
PMID: 22503819

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146270 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (8 distinct):
T-complex protein 1 subunit zeta Chains: F, N, f, n
Molecule details ›
Chains: F, N, f, n
Length: 546 amino acids
Theoretical weight: 60 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P39079 (Residues: 1-546; Coverage: 100%)
Gene names: CCT6, TCP20, TCP6, YD9395.21, YDR188W
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit theta Chains: H, P, h, p
Molecule details ›
Chains: H, P, h, p
Length: 568 amino acids
Theoretical weight: 61.74 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P47079 (Residues: 1-568; Coverage: 100%)
Gene names: CCT8, J1374, YJL008C
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit eta Chains: G, O, g, o
T-complex protein 1 subunit epsilon Chains: E, M, e, m
T-complex protein 1 subunit beta Chains: B, J, b, j
T-complex protein 1 subunit delta Chains: D, L, d, l
T-complex protein 1 subunit alpha Chains: A, I, a, i
T-complex protein 1 subunit gamma Chains: C, K, c, k

Ligands and Environments

3 bound ligands:
Ligand MG 32 x MG
Ligand ADP 32 x ADP
Ligand BEF 32 x BEF
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P1
Unit cell:
a: 159.1Å b: 162.54Å c: 268.1Å
α: 85.23° β: 81.15° γ: 61.17°
R-values:
R R work R free
0.259 0.257 0.305
Expression system: Saccharomyces cerevisiae

Quick links

Citations

33 review citations

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

13 mentions without citation

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