3E2J: Crystal Structure Of Bovine Coupling Factor B

Coupling factor B (FB) is a mitochondrial inner membrane polypeptide that facilitates the energy-driven catalysis of ATP synthesis in animal mitochondria by blocking a proton leak across the membrane. Here, we report the crystal structure of the bovine mitochondrial FB mutant with Gly-3-Glu substitution determined at a resolution of 0.96 A and that of the WT polypeptide at a resolution of 2.9 A. The structure reveals an oblong, oval-shaped molecule with a unique globular N-terminal domain that is proposed to be the membrane anchor domain and the capping region to the C-terminal leucine-rich repeats domain. A short N-terminal alpha-helix, which extends away from the molecule's body, is suggestive of functioning as an anchor for FB to the matrix side of the mitochondrial inner membrane. Identification of a bound Mg(2+) ion reveals that FB is a metalloprotein. We also report the cocrystal structures of FB bound with phenylarsine oxide and Cd(2+), two known inhibitors of the FB coupling activity.
PDB ID: 3E2JDownload
MMDB ID: 66220
PDB Deposition Date: 2008/8/5
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3E2J: monomeric; determined by author and by software (PISA)
Molecular Components in 3E2J
Label Count Molecule
Protein (1 molecule)
ATP Synthase Subunit S, Mitochondrial(Gene symbol: ATP5S)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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