Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance
Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance
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DOI：
10.7554/elife.56862
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发表时间：
2020-07-08
期刊：
影响因子：
7.7
通讯作者：
Yokoyama, Ken
中科院分区：
文献类型：
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作者：
Kishikawa, Jun-ichi;Nakanishi, Atsuko;Yokoyama, Ken
v -ATP酶是一种能量转换酶，在亲水的V-1结构域中偶联ATP水解/合成，质子通过V-o膜结构域，通过中心转子复合物相对于周围定子装置的旋转。在与V-1结构域解离后，真核v - atp酶的V-o结构域可以采取生理上相关的自抑制形式，阻止质子通过V-o结构域的传导，然而这种抑制的分子机制尚不完全清楚。利用低温电子显微镜，我们分别在近原子分辨率下确定了全息V/ a - atp酶和分离的V-o的结构。这些结构阐明了孤立的V-o结构域是如何采用自抑制形式的，以及holo配合物是如何阻止抑制V-o形式的形成的。
V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V-1 domain, with proton flow through the V-o membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V-1 domain, the V-o domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the V-o 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 V-o at near-atomic resolution, respectively. These structures clarify how the isolated V-o domain adopts the auto-inhibited form and how the holo complex prevents formation of the inhibited V-o form.