› 6ynv

Electron Microscopy
2.8Å resolution

Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-wing region

Released:
DOI: 10.2210/pdb6ynv/pdb
PDB entry 6ynv coloured by chain, front view.
PDB entry 6ynv coloured by chain, side view.
PDB entry 6ynv coloured by chain, top view.
Source organism: Tetrahymena thermophila
Primary publication:
Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
Flygaard RK, Mühleip A, Tobiasson V, Amunts A
OpenAccess logo Nat Commun 11 5342 (2020)
PMID: 33093501
Related structures: EMD-10857

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD/NAD(P)-binding domain-containing protein Chain: e
Molecule details ›
Chain: e
Length: 480 amino acids
Theoretical weight: 54.92 KDa
Source organism: Tetrahymena thermophila
UniProt:
  • Canonical: I7LVQ8 (Residues: 1-480; Coverage: 100%)
Gene name: TTHERM_00137990
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase

Ligands and Environments

1 bound ligand:
Ligand NAD 1 x NAD
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 2.8Å
Relevant EMDB volumes: EMD-10857

Quick links

Citations

5 review citations

Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions.
Bernardi et al. (2023)
4 more