3E4G

Crystal structure of bovine coupling Factor B, G28E mutant

3E4G の概要

• エントリーDOI: 10.2210/pdb3e4g/pdb
• 関連するPDBエントリー: 3DZE 3E2J 3E3Z
• 分子名称: ATP synthase subunit s, mitochondrial, MAGNESIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: leucine-rich repeat, cf0, hydrogen ion transport, inner membrane, ion transport, membrane, mitochondrion, transit peptide, transport, electron transport
• 由来する生物種: Bos taurus
• 細胞内の位置: Mitochondrion: P22027
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20661.19

構造登録者

Stroud, R.M.,Lee, J.K.,Belogrudov, G.I. (登録日: 2008-08-11, 公開日: 2008-08-26, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (0.96 Å)