3OEH

Structure of four mutant forms of yeast F1 ATPase: beta-V279F

3OEH の概要

• エントリーDOI: 10.2210/pdb3oeh/pdb
• 関連するPDBエントリー: 1W0J 2HLD 3FKS 3OE7 3OEE 3OFN
• 分子名称: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (7 entities in total)
• 機能のキーワード: atp synthase, atp phosphatase, f1f0 atpase, atp synthesis, hydrolase, adp, po4, mitochondria
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); 詳細
• 細胞内の位置: Mitochondrion inner membrane: P07251; Mitochondrion: P00830 P38077 Q12165 P21306
• タンパク質・核酸の鎖数: 27
• 化学式量合計: 1127068.92

構造登録者

Arsenieva, D.,Symersky, J.,Wang, Y.,Pagadala, V.,Mueller, D.M. (登録日: 2010-08-12, 公開日: 2010-09-15, 最終更新日: 2023-09-06)

主引用文献

Arsenieva, D.,Symersky, J.,Wang, Y.,Pagadala, V.,Mueller, D.M.
Crystal structures of mutant forms of the yeast f1 ATPase reveal two modes of uncoupling.
J.Biol.Chem., 285:36561-36569, 2010

PubMed Abstract: The mitochondrial ATP synthase couples the flow of protons with the phosphorylation of ADP. A class of mutations, the mitochondrial genome integrity (mgi) mutations, has been shown to uncouple this process in the yeast mitochondrial ATP synthase. Four mutant forms of the yeast F(1) ATPase with mgi mutations were crystallized; the structures were solved and analyzed. The analysis identifies two mechanisms of structural uncoupling: one in which the empty catalytic site is altered and in doing so, apparently disrupts substrate (phosphate) binding, and a second where the steric hindrance predicted between γLeu83 and β(DP) residues, Leu-391 and Glu-395, located in Catch 2 region, is reduced allowing rotation of the γ-subunit with less impedance. Overall, the structures provide key insights into the critical interactions in the yeast ATP synthase involved in the coupling process.

PubMed: 20843806
DOI: 10.1074/jbc.M110.174383

実験手法

X-RAY DIFFRACTION (3 Å)