2QE7

Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1

2QE7 の概要

• エントリーDOI: 10.2210/pdb2qe7/pdb
• 関連するPDBエントリー: 1JNV 1SKY
• 分子名称: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (4 entities in total)
• 機能のキーワード: blockage of atp hydrolysis, f1-atpase, atp synthase, single particle analysis, thermoalkaliphilic, hydrolase
• 由来する生物種: Bacillus sp.; 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein (By similarity): Q71CG5 Q71CG3 Q71CG4 Q71CG2
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 362763.77

構造登録者

Stocker, A.,Keis, S.,Vonck, J.,Cook, G.M.,Dimroth, P. (登録日: 2007-06-25, 公開日: 2007-08-21, 最終更新日: 2023-08-30)

主引用文献

Stocker, A.,Keis, S.,Vonck, J.,Cook, G.M.,Dimroth, P.
The Structural Basis for Unidirectional Rotation of Thermoalkaliphilic F(1)-ATPase.
Structure, 15:904-914, 2007

PubMed Abstract: The ATP synthase of the thermoalkaliphilic Bacillus sp. TA2.A1 operates exclusively in ATP synthesis direction. In the crystal structure of the nucleotide-free alpha(3)beta(3)gamma epsilon subcomplex (TA2F(1)) at 3.1 A resolution, all three beta subunits adopt the open beta(E) conformation. The structure shows salt bridges between the helix-turn-helix motif of the C-terminal domain of the beta(E) subunit (residues Asp372 and Asp375) and the N-terminal helix of the gamma subunit (residues Arg9 and Arg10). These electrostatic forces pull the gamma shaft out of the rotational center and impede rotation through steric interference with the beta(E) subunit. Replacement of Arg9 and Arg10 with glutamines eliminates the salt bridges and results in an activation of ATP hydrolysis activity, suggesting that these salt bridges prevent the native enzyme from rotating in ATP hydrolysis direction. A similar bending of the gamma shaft as in the TA2F(1) structure was observed by single-particle analysis of the TA2F(1)F(o) holoenzyme.

PubMed: 17697996
DOI: 10.1016/j.str.2007.06.009

実験手法

X-RAY DIFFRACTION (3.06 Å)