› 8tpl

Electron Microscopy
3.46Å resolution

ATP-2 state of Bcs1 (unsymmetrized)

Released:
DOI: 10.2210/pdb8tpl/pdb
PDB entry 8tpl coloured by chain, front view.
PDB entry 8tpl coloured by chain, side view.
PDB entry 8tpl coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate.
Zhan J, Zeher A, Huang R, Tang WK, Jenkins LM, Xia D
Nat Commun 15 4655 (2024)
PMID: 38821922
Related structures: EMD-41476

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190030 (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: 427 amino acids
Theoretical weight: 48.66 KDa
Source organism: Mus musculus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9CZP5 (Residues: 1-418; Coverage: 100%)
Gene name: Bcs1l
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 7 x ATP
Ligand MG 7 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.46Å
Relevant EMDB volumes: EMD-41476
Expression system: Komagataella pastoris

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