Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6085, USA.
Annu Rev Biophys. 2010;39:539-57. doi: 10.1146/annurev.biophys.050708.133751.
The general structural features of the motor region of myosin superfamily members are now well established, as is a subset of the structural and kinetic transitions of the actin-myosin catalytic cycle. Not yet visualized are the structural rearrangements triggered by actin binding that are coupled to force generation and product release. In this review we describe the recent progress in understanding these missing components of the mechanism of chemomechanical transduction by myosin motors. These insights come from a combination of kinetic and single-molecule studies on multiple classes of myosins, with additional insights from contracting muscle fibers. These recent studies have explored the effects of intermediate and high loads on the kinetics of the actin-bound myosin state transitions. We also describe studies that delineate how some classes of myosin motors are adapted for processive movement on actin.
肌球蛋白超家族成员的运动区域的一般结构特征现在已经确立，肌球蛋白的结构和动力学转变的一个子集也已经确立，但是actin 结合引发的结构重排与力的产生和产物释放偶联的结构重排还没有被可视化。在这篇综述中，我们描述了最近在理解肌球蛋白马达的化学机械转导机制中这些缺失成分方面的进展。这些见解来自于对多种肌球蛋白的动力学和单分子研究的结合，以及来自收缩肌纤维的额外见解。这些最近的研究探讨了中间和高负荷对肌球蛋白结合肌动蛋白状态转变动力学的影响。我们还描述了一些肌球蛋白如何适应在肌动蛋白上进行连续运动的研究。
