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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure of dimeric mitochondrial ATP synthase: Novel F-0 bridging features and the structural basis of mitochondrial cristae biogenesis
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Structure of dimeric mitochondrial ATP synthase: Novel F-0 bridging features and the structural basis of mitochondrial cristae biogenesis

机译：二聚体线粒体ATP合酶的结构：新型F-0桥接特征和线粒体cr生物的结构基础

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摘要

The F1F0-ATP synthase exists as a dimer in mitochondria, where it is essential for the biogenesis of the inner membrane cristae. How two ATP synthase complexes dimerize to promote cristae formation is unknown. Here we resolved the structure of the dimeric F1F0 ATP synthase complex isolated from bovine heart mitochondria by transmission electron microscopy. The structure of the ATP synthase dimer has an overall conic appearance that is consistent with the proposed role of the dimeric enzyme in mitochondrial cristae biogenesis. The ATP synthase dimer interface is formed by contacts on both the F-0 and F-1 domains. A cross-bridging protein density was resolved which connects the two F-0 domains on the intermembrane space side of the membrane. On the matrix side of the complex, the two F-1 moieties are connected by a protein bridge, which is attributable to the IF1 inhibitor protein.
机译：F1F0-ATP合酶在线粒体中以二聚体形式存在，在那里对于内膜cr的生物发生至关重要。尚不清楚两个ATP合酶复合物如何二聚化以促进cr的形成。在这里，我们通过透射电子显微镜解析了从牛心脏线粒体分离的二聚体F1F0 ATP合酶复合物的结构。 ATP合酶二聚体的结构总体呈圆锥形，与二聚体酶在线粒体cr生物发生中的拟议作用一致。 ATP合酶二聚体界面由F-0和F-1域上的接触形成。解析了一种跨桥蛋白密度，该密度将膜的膜内空间侧的两个F-0域连接在一起。在复合物的基质侧，两个F-1部分通过蛋白质桥连接，这可归因于IF1抑制剂蛋白质。

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