› 6sh4

Electron Microscopy
4.4Å resolution

Structure of the Apo1 state of the heptameric Bcs1 AAA-ATPase.

Released:
DOI: 10.2210/pdb6sh4/pdb
PDB entry 6sh4 coloured by chain, front view.
PDB entry 6sh4 coloured by chain, side view.
PDB entry 6sh4 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.
Kater L, Wagener N, Berninghausen O, Becker T, Neupert W, Beckmann R
Nat Struct Mol Biol 27 142-149 (2020)
PMID: 31988523
Related structures: EMD-10193

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152469 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial chaperone BCS1 Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 456 amino acids
Theoretical weight: 51.17 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P32839 (Residues: 1-456; Coverage: 100%)
Gene names: BCS1, D9481.17, YDR375C
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.4Å
Relevant EMDB volumes: EMD-10193

Quick links

Citations

7 review citations

Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions.
Protasoni et al. (2021)
6 more

2 mentions without citation

Structural snapshots of the cellular folded protein translocation machinery Bcs1.
Xia D. (2021)
1 more