Ministry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
SUSTech Cryo-EM Facility Center, Southern University of Science and Technology, Shenzhen 518055, China.
Science. 2019 Jun 14;364(6445):1068-1075. doi: 10.1126/science.aaw4852.
The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-Å resolution.
线粒体三磷酸腺苷（ATP）合酶产生哺乳动物细胞所需的大部分 ATP。我们分离了猪四聚体 ATP 合酶，并使用单颗粒冷冻电子显微镜方法在 6.2 埃的分辨率下解决了其结构。从基质侧观察，两个经典的 V 形 ATP 合酶二聚体彼此呈反平行排列，形成 H 形 ATP 合酶四聚体。ATP 合酶抑制因子亚基 1（IF1）是一种在低 pH 下已知的哺乳动物 ATP 合酶的体内抑制剂。两个 IF1 二聚体连接两个 ATP 合酶二聚体，这与 ATP 合酶四聚体采用抑制状态一致。在四聚体中，我们在 3.34- 和 3.45-Å 分辨率下对两种不同旋转构象的完整 ATP 合酶结构进行了细化。
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