Structure of a bacterial ATP synthase
Structure of a bacterial ATP synthase
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DOI：
10.7554/elife.43128
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发表时间：
2019-02-06
期刊：
影响因子：
7.7
通讯作者：
Rubinstein, John L.
中科院分区：
文献类型：
--
作者：
Guo, Hui;Suzuki, Toshiharu;Rubinstein, John L.
ATP酶利用来自跨膜质子动力的能量从ADP和无机磷酸盐产生ATP。细菌ATP酶已被广泛研究，因为它们是酶的最简单形式，并且因为这些复合物的遗传操作相对容易。我们表达的芽孢杆菌PS3 ATP合酶在土着大肠杆菌，纯化，并通过冷冻电镜成像，使我们能够建立原子模型的复杂的三个旋转状态。亚基的位置显示了它如何能够抑制ATP水解，同时允许ATP合成。膜区域的结构显示了简单的细菌ATP合酶如何能够执行与等效但更复杂的线粒体复合物相同的核心功能。这些结构揭示了跨膜质子转运的路径，并为理解数十年来对酶中特定残基作用的生化分析提供了一个模型。
ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit epsilon shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme.