› 7ttt

Electron Microscopy
2.9Å resolution

The beta-tubulin folding intermediate III

Released:
DOI: 10.2210/pdb7ttt/pdb
PDB entry 7ttt coloured by chain, front view.
PDB entry 7ttt coloured by chain, side view.
PDB entry 7ttt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
Gestaut D, Zhao Y, Park J, Ma B, Leitner A, Collier M, Pintilie G, Roh SH, Chiu W, Frydman J
Cell 185 4770-4787.e20 (2022)
PMID: 36493755
Related structures: EMD-26123

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
PDBe Complex ID:
PDB-CPX-139587 (preferred)
Entry contents:
9 distinct polypeptide molecules
Macromolecules (9 distinct):
Tubulin beta chain Chain: A
Molecule details ›
Chain: A
Length: 444 amino acids
Theoretical weight: 49.72 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P07437 (Residues: 1-444; Coverage: 100%)
Gene names: OK/SW-cl.56, TUBB, TUBB5
Sequence domains:
T-complex protein 1 subunit theta Chain: B
Molecule details ›
Chain: B
Length: 547 amino acids
Theoretical weight: 59.58 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P50990 (Residues: 1-547; Coverage: 100%)
Gene names: C21orf112, CCT8, CCTQ, KIAA0002
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit eta Chain: C
Molecule details ›
Chain: C
Length: 553 amino acids
Theoretical weight: 60.56 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q99832 (Residues: 1-471, 472-543; Coverage: 100%)
Gene names: CCT7, CCTH, NIP7-1
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit epsilon Chain: D
Molecule details ›
Chain: D
Length: 541 amino acids
Theoretical weight: 59.75 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P48643 (Residues: 1-541; Coverage: 100%)
Gene names: CCT5, CCTE, KIAA0098
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit beta Chain: E
Molecule details ›
Chain: E
Length: 535 amino acids
Theoretical weight: 57.57 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
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 delta Chain: F
Molecule details ›
Chain: F
Length: 539 amino acids
Theoretical weight: 58 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
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 alpha Chain: G
Molecule details ›
Chain: G
Length: 556 amino acids
Theoretical weight: 60.42 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P17987 (Residues: 1-556; Coverage: 100%)
Gene names: CCT1, CCTA, TCP1
Sequence domains: TCP-1/cpn60 chaperonin family
T-complex protein 1 subunit gamma Chain: H
Molecule details ›
Chain: H
Length: 545 amino acids
Theoretical weight: 60.61 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
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 zeta Chain: I
Molecule details ›
Chain: I
Length: 531 amino acids
Theoretical weight: 58.17 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P40227 (Residues: 1-531; Coverage: 100%)
Gene names: CCT6, CCT6A, CCTZ
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

3 bound ligands:
Ligand MG 8 x MG
Ligand ADP 8 x ADP
Ligand AF3 8 x AF3
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-26123
Expression system: Trichoplusia ni

Quick links

Citations

5 review citations

Mechanisms and pathology of protein misfolding and aggregation.
Louros et al. (2023)
4 more

1 mention without citation

Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
Gestaut et al. (2022)