Molecular Architecture of the Rotary Motor in ATP Synthase

作者：Daniela Stock, Andrew G. W. Leslie, John E. Walker · 发表于：Science · 年份：1999 · DOI：10.1126/science.286.5445.1700 · 被引用次数：1271 · 研究领域：ATP Synthase and ATPases Research、Mitochondrial Function and Pathology、Photosynthetic Processes and Mechanisms

Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.