The molecular structure of an axle-less F1-ATPase

Emily J. Furlong, Ian-Blaine P. Reininger-Chatzigiannakis, Yi C. Zeng, Simon H. J. Brown, Meghna Sobti, Alastair G. Stewart
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Abstract

F1Fo ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F1-ATPase catalytic cores can hydrolyse ATP, passing through a series of conformational states involving rotation of the central γ rotor subunit and the opening and closing of the catalytic β subunits. Cooperativity in F1-ATPase has long thought to be conferred through the γ subunit, with three key interaction sites between the γ and β subunits being identified. Single molecule studies have demonstrated that the F1 complexes lacking the γ axle still “rotate” and hydrolyse ATP, but with less efficiency. We solved the cryogenic electron microscopy structure of an axle-less Bacillus sp. PS3 F1-ATPase. The unexpected binding-dwell conformation of the structure in combination with the observed lack of interactions between the axle-less γ and the open β subunit suggests that the complete γ subunit is important for coordinating efficient ATP binding of F1-ATPase.
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无轴 F1-ATP 酶的分子结构
F1Fo ATP 合酶是一种分子旋转马达,可利用跨膜质子动力产生 ATP。分离的 F1-ATP 酶催化核心可以水解 ATP,并通过一系列构象状态,包括中心 γ 转子亚基的旋转和催化 β 亚基的开合。长期以来,人们一直认为 F1-ATP 酶的协同作用是通过 γ 亚基实现的,并已发现 γ 和 β 亚基之间有三个关键的相互作用位点。单分子研究表明,缺少γ轴的F1复合物仍能 "旋转 "并水解ATP,但效率较低。我们解决了无轴芽孢杆菌 PS3 F1-ATP 酶的低温电子显微镜结构。该结构意想不到的结合-停留构象,以及观察到的无轴γ和开放β亚基之间缺乏相互作用的现象表明,完整的γ亚基对于协调F1-ATP酶有效的ATP结合非常重要。
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