Rayment I, Holden H M, Whittaker M, Yohn C B, Lorenz M, Holmes K C, Milligan R A
Department of Biochemistry, University of Wisconsin, Madison 53705.
Science. 1993 Jul 2;261(5117):58-65. doi: 10.1126/science.8316858.
Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.
肌肉收缩由肌球蛋白和肌动蛋白之间的周期性相互作用组成，这种相互作用由三磷酸腺苷（ATP）的伴随水解驱动。通过将单个蛋白质的分子结构与通过冷冻电子显微镜和图像分析获得的复合物的低分辨率电子密度图相结合，得到了F肌动蛋白和肌球蛋白头部的僵直复合物模型。肌球蛋白上的ATP结合口袋与肌动蛋白上的主要接触区域之间的空间关系为横桥循环提出了一个工作假设，该假设与先前独立的结构和生化研究一致。
