› 7k59

Electron Microscopy
4.2Å resolution

Structure of apo VCP hexamer generated from bacterially recombinant VCP/p97

Released:
DOI: 10.2210/pdb7k59/pdb
PDB entry 7k59 coloured by chain, front view.
PDB entry 7k59 coloured by chain, side view.
PDB entry 7k59 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation.
Yu G, Bai Y, Li K, Amarasinghe O, Jiang W, Zhang ZY
OpenAccess logo iScience 24 103310 (2021)
PMID: 34765927
Related structures: EMD-22678

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transitional endoplasmic reticulum ATPase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 806 amino acids
Theoretical weight: 89.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55072 (Residues: 1-806; Coverage: 100%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 4.2Å
Relevant EMDB volumes: EMD-22678
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The functional importance of VCP to maintaining cellular protein homeostasis.
Ahlstedt et al. (2022)
1 more

2 mentions without citation

Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation.
Yu et al. (2021)
1 more