› 2xqu

X-ray diffraction
1.84Å resolution

Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases

Released:
DOI: 10.2210/pdb2xqu/pdb
PDB entry 2xqu coloured by chain, front view.
PDB entry 2xqu coloured by chain, side view.
PDB entry 2xqu coloured by chain, top view.
Source organism: Arthrospira platensis
Primary publication:
Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases.
Pogoryelov D, Krah A, Langer JD, Yildiz Ö, Faraldo-Gómez JD, Meier T
Nat Chem Biol 6 891-9 (2010)
PMID: 20972431

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP SYNTHASE C CHAIN Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 82 amino acids
Theoretical weight: 8.21 KDa
Source organism: Arthrospira platensis
Structure domains: F1F0 ATP synthase subunit C

Ligands and Environments

1 bound ligand:
Ligand CVM 55 x CVM
1 modified residue:
Ligand FME 5 x FME

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6322
Unit cell:
a: 93.89Å b: 93.89Å c: 257.32Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.189 0.224

Quick links

Citations

21 review citations

ATP synthase.
Junge et al. (2015)
20 more

2 mentions without citation

Single-molecule analysis of F0F1-ATP synthase inhibited by N,N-dicyclohexylcarbodiimide.
Toei et al. (2013)
1 more