1] Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK. [2] Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Nat Rev Mol Cell Biol. 2013 Nov;14(11):713-26. doi: 10.1038/nrm3667. Epub 2013 Sep 25.
Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how these giant motor proteins work. From these studies, a model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.
在 ATP 水解的推动下，动力蛋白在许多生物过程中（包括纤毛运动、细胞分裂和细胞内运输）在微管上产生力和运动。动力蛋白马达的巨大质量和复杂性使得阐明其机制成为一项艰巨的任务。然而，通过 X 射线晶体学、低温电子显微镜、单分子测定和生化实验等多种方法的结合，在理解这些巨型马达蛋白如何工作方面已经取得了重要进展。从这些研究中，动力蛋白的机械化学循环模型正在出现，其中核苷酸驱动的动力蛋白 AAA+环内的弯曲运动改变了其微管结合臂的亲和力，并重塑其机械元件以产生运动。
