› 4v1g

X-ray diffraction
1.55Å resolution

Crystal structure of a mycobacterial ATP synthase rotor ring

Released:
DOI: 10.2210/pdb4v1g/pdb
PDB entry 4v1g coloured by chain, front view.
PDB entry 4v1g coloured by chain, side view.
PDB entry 4v1g coloured by chain, top view.
Source organism: Mycolicibacterium phlei
Primary publication:
Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline.
Preiss L, Langer JD, Yildiz Ö, Eckhardt-Strelau L, Guillemont JE, Koul A, Meier T
OpenAccess logo Sci Adv 1 e1500106 (2015)
PMID: 26601184

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
F0F1 ATP SYNTHASE SUBUNIT C Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 86 amino acids
Theoretical weight: 8.61 KDa
Source organism: Mycolicibacterium phlei
Structure domains: F1F0 ATP synthase subunit C

Ligands and Environments

1 bound ligand:
Ligand BOG 3 x BOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: R3
Unit cell:
a: 73.67Å b: 73.67Å c: 166.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.158 0.18

Quick links

Citations

32 review citations

Structure and Mechanisms of F-Type ATP Synthases.
Kühlbrandt W. (2019)
31 more

4 mentions without citation

The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation.
Ragunathan et al. (2017)
3 more