3DZE

Crystal structure of bovine coupling Factor B bound with cadmium

Summary for 3DZE

• Entry DOI: 10.2210/pdb3dze/pdb
• Related: 3E2J 3E3Z 3E4G
• Descriptor: ATP synthase subunit s, mitochondrial, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CADMIUM ION, ... (5 entities in total)
• Functional Keywords: leucine-rich repeat, cf(0), hydrogen ion transport, ion transport, membrane, mitochondrion, mitochondrion inner membrane, transit peptide, transport, transport protein, electron transport
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• Cellular location: Mitochondrion: P22027
• Total number of polymer chains: 1
• Total formula weight: 20773.60

Authors

Lee, J.K.,Stroud, R.M.,Belogrudov, G.I. (deposition date: 2008-07-29, release date: 2008-08-19, Last modification date: 2024-02-21)

Primary citation

Lee, J.K.,Belogrudov, G.I.,Stroud, R.M.
Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.
Proc.Natl.Acad.Sci.Usa, 105:13379-13384, 2008

PubMed Abstract: 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.

PubMed: 18768789
DOI: 10.1073/pnas.0805689105

Experimental method

X-RAY DIFFRACTION (1.15 Å)