Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded FOregion turns the rotor that drives ATP synthesis in the soluble F1region. Although crystal structures of the F1region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the FOregion. Using cryo–electron microscopy, we determined the structure of the dimeric FOcomplex fromSaccharomyces cerevisiaeat a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae.

中文翻译：

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线粒体ATP合酶二聚体FO区的原子模型

线粒体三磷酸腺苷（ATP）合酶在真核细胞中产生大多数ATP，其二聚化对于产生线粒体特有的内膜褶皱或cr是必要的。质子通过膜嵌入的FO区域易位，使转子驱动可溶性F1区域中的ATP合成。尽管F1区的晶体结构已经说明了这种旋转是如何导致ATP合成的，但由于缺少FO区的实验性原子模型，因此难以理解质子易位是如何产生旋转的。使用冷冻电子显微镜，我们确定了酿酒酵母中二聚体FOcomplex的结构，分辨率为3.6埃。该结构阐明了质子如何穿过复合物，复合物如何二聚化，