› 6f0x

Electron Microscopy
4.6Å resolution

Cryo-EM structure of TRIP13 in complex with ATP gamma S, p31comet, C-Mad2 and Cdc20

Released:
DOI: 10.2210/pdb6f0x/pdb
PDB entry 6f0x coloured by chain, front view.
PDB entry 6f0x coloured by chain, side view.
PDB entry 6f0x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanism for remodelling of the cell cycle checkpoint protein MAD2 by the ATPase TRIP13.
Alfieri C, Chang L, Barford D
Nature (2018)
PMID: 29973720
Related structures: EMD-4166

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-171410 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Pachytene checkpoint protein 2 homolog Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 432 amino acids
Theoretical weight: 48.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15645 (Residues: 1-432; Coverage: 100%)
Gene names: PCH2, TRIP13
Sequence domains: ATPase family associated with various cellular activities (AAA)
MAD2L1-binding protein Chain: P
Molecule details ›
Chain: P
Length: 274 amino acids
Theoretical weight: 31.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15013 (Residues: 1-274; Coverage: 100%)
Gene names: CMT2, KIAA0110, MAD2L1BP
Sequence domains: Mad1 and Cdc20-bound-Mad2 binding
Cell division cycle protein 20 homolog Chain: Q
Molecule details ›
Chain: Q
Length: 499 amino acids
Theoretical weight: 54.8 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q12834 (Residues: 1-499; Coverage: 100%)
Gene name: CDC20
Sequence domains:
Mitotic spindle assembly checkpoint protein MAD2A Chain: Z
Molecule details ›
Chain: Z
Length: 205 amino acids
Theoretical weight: 23.53 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q13257 (Residues: 1-205; Coverage: 100%)
Gene names: MAD2, MAD2L1
Sequence domains: HORMA domain

Ligands and Environments

1 bound ligand:
Ligand AGS 5 x AGS
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.6Å
Relevant EMDB volumes: EMD-4166
Expression systems:
  • Escherichia coli
  • Trichoplusia ni

Quick links

Citations

17 review citations

The molecular principles governing the activity and functional diversity of AAA+ proteins.
Puchades et al. (2020)
16 more

8 mentions without citation

Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.
Gates et al. (2020)
7 more