› 5vc7

Electron Microscopy
3.9Å resolution

VCP like ATPase from T. acidophilum (VAT) - conformation 1

Released:
DOI: 10.2210/pdb5vc7/pdb
PDB entry 5vc7 coloured by chain, front view.
PDB entry 5vc7 coloured by chain, side view.
PDB entry 5vc7 coloured by chain, top view.
Source organism: Thermoplasma acidophilum DSM 1728
Primary publication:
Structure of a AAA+ unfoldase in the process of unfolding substrate.
Ripstein ZA, Huang R, Augustyniak R, Kay LE, Rubinstein JL
Elife 6 (2017)
PMID: 28390173
Related structures: EMD-8658

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126471 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
VCP-like ATPase Chains: A, C, D, E, F, G
Molecule details ›
Chains: A, C, D, E, F, G
Length: 564 amino acids
Theoretical weight: 63 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O05209 (Residues: 183-745; Coverage: 76%)
Gene names: Ta0840, vat
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ATP 12 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.9Å
Relevant EMDB volumes: EMD-8658
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

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

4 mentions without citation

AAA-ATPases in Protein Degradation.
Yedidi et al. (2017)
3 more