V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo domain adopts the auto-inhibited form and how the holo complex prevents formation of the inhibited Vo form.

中文翻译：

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来自 V/A-ATPase 的分离 Vo 的机械抑制用于质子传导

V-ATPase 是一种能量转换酶，通过中心转子复合体相对于周围定子装置的旋转，将亲水性 V1 域中的 ATP 水解/合成与质子流通过 Vo 膜域相耦合。从 V1 结构域解离后，真核生物 V-ATPase 的 Vo 结构域可以采用生理相关的自动抑制形式，其中通过 Vo 结构域的质子传导被阻止，但是这种抑制的分子机制尚不完全清楚。使用低温电子显微镜，我们分别以近原子分辨率确定了全息 V/A-ATPase 和孤立 Vo 的结构。这些结构阐明了孤立的 Vo 结构域如何采用自动抑制形式以及全息复合物如何防止形成受抑制的 Vo 形式。