› 7x0v

Electron Microscopy
3.2Å resolution

cryo-EM structure of human TRiC-ADP-AlFx

Released:
DOI: 10.2210/pdb7x0v/pdb
PDB entry 7x0v coloured by chain, front view.
PDB entry 7x0v coloured by chain, side view.
PDB entry 7x0v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Liu C, Jin M, Wang S, Han W, Zhao Q, Wang Y, Xu C, Diao L, Yin Y, Peng C, Bao L, Wang Y, Cong Y
OpenAccess logo Commun Biol 6 531 (2023)
PMID: 37193829
Related structures: EMD-32926

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-148234 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (8 distinct):
T-complex protein 1 subunit zeta Chains: K, z
Molecule details ›
Chains: K, z
Length: 531 amino acids
Theoretical weight: 58.11 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P40227 (Residues: 1-531; Coverage: 100%)
Gene names: CCT6, CCT6A, CCTZ
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit theta Chains: J, P
Molecule details ›
Chains: J, P
Length: 548 amino acids
Theoretical weight: 59.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P50990 (Residues: 1-548; Coverage: 100%)
Gene names: C21orf112, CCT8, CCTQ, KIAA0002
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit eta Chains: H, O
Molecule details ›
Chains: H, O
Length: 543 amino acids
Theoretical weight: 59.42 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q99832 (Residues: 1-543; Coverage: 100%)
Gene names: CCT7, CCTH, NIP7-1
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit gamma Chains: G, N
Molecule details ›
Chains: G, N
Length: 545 amino acids
Theoretical weight: 60.61 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P49368 (Residues: 1-545; Coverage: 100%)
Gene names: CCT3, CCTG, TRIC5
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit epsilon Chains: E, e
Molecule details ›
Chains: E, e
Length: 539 amino acids
Theoretical weight: 59.55 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P48643 (Residues: 3-541; Coverage: 100%)
Gene names: CCT5, CCTE, KIAA0098
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit delta Chains: I, M
Molecule details ›
Chains: I, M
Length: 539 amino acids
Theoretical weight: 58 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P50991 (Residues: 1-539; Coverage: 100%)
Gene names: CCT4, CCTD, SRB
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit beta Chains: B, L
Molecule details ›
Chains: B, L
Length: 535 amino acids
Theoretical weight: 57.57 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P78371 (Residues: 1-535; Coverage: 100%)
Gene names: 99D8.1, CCT2, CCTB
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit alpha Chains: A, a
Molecule details ›
Chains: A, a
Length: 556 amino acids
Theoretical weight: 60.42 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P17987 (Residues: 1-556; Coverage: 100%)
Gene names: CCT1, CCTA, TCP1
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

3 bound ligands:
Ligand ADP 16 x ADP
Ligand MG 16 x MG
Ligand AF3 16 x AF3
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.2Å
Relevant EMDB volumes: EMD-32926
Expression system: Homo sapiens

Quick links

Citations

3 review citations

Balancing Act: Tubulin Glutamylation and Microtubule Dynamics in Toxoplasma gondii.
Delgado et al. (2024)
2 more

1 mention without citation

Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Liu et al. (2023)