› 5vca

Electron Microscopy
4.8Å resolution

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

Released:
DOI: 10.2210/pdb5vca/pdb
PDB entry 5vca coloured by chain, front view.
PDB entry 5vca coloured by chain, side view.
PDB entry 5vca 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
OpenAccess logo Elife 6 (2017)
PMID: 28390173
Related structures: EMD-8659

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: M, N, O, P, Q, R
Molecule details ›
Chains: M, N, O, P, Q, R
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.8Å
Relevant EMDB volumes: EMD-8659
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

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

4 mentions without citation

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