Kinesins are a diverse group of adenosine triphosphate (ATP)‐dependent motor proteins that transport cargos along microtubules (MTs) and change the organization of MT networks. Shared among all kinesins is a ~40 kDa motor domain that has evolved an impressive assortment of motility and MT remodeling mechanisms as a result of subtle tweaks and edits within its sequence. Several elegant studies of different kinesin isoforms have exposed the purpose of structural changes in the motor domain as it engages and leaves the MT. However, few studies have compared the sequences and MT contacts of these kinesins systematically. Along with clever strategies to trap kinesin–tubulin complexes for X‐ray crystallography, new advancements in cryo‐electron microscopy have produced a burst of high‐resolution structures that show kinesin–MT interfaces more precisely than ever. This review considers the MT interactions of kinesin subfamilies that exhibit significant differences in speed, processivity, and MT remodeling activity. We show how their sequence variations relate to their tubulin footprint and, in turn, how this explains the molecular activities of previously characterized mutants. As more high‐resolution structures become available, this type of assessment will quicken the pace toward establishing each kinesin's design–function relationship.

中文翻译：

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这些马达是为行走而制造的。

驱动蛋白是一组多样化的三磷酸腺苷 (ATP) 依赖性运动蛋白，可沿微管 (MT) 运输货物并改变 MT 网络的组织。在所有驱动蛋白之间共享的是一个约 40 kDa 的运动域，由于其序列中的细微调整和编辑，该域已经进化出一系列令人印象深刻的运动和 MT 重塑机制。对不同驱动蛋白同种型的几项优雅研究揭示了运动域在参与和离开 MT 时结构变化的目的。然而，很少有研究系统地比较这些驱动蛋白的序列和 MT 接触。除了为 X 射线晶体学捕获驱动蛋白-微管蛋白复合物的巧妙策略外，冷冻电子显微镜的新进展产生了一系列高分辨率结构，比以往更精确地显示驱动蛋白-MT 界面。本综述考虑了在速度、持续合成能力和 MT 重塑活动方面表现出显着差异的驱动蛋白亚家族的 MT 相互作用。我们展示了它们的序列变异如何与它们的微管蛋白足迹相关，反过来，这又如何解释了先前表征突变体的分子活动。随着更多高分辨率结构的出现，这种类型的评估将加快建立每个驱动蛋白的设计-功能关系的步伐。我们展示了它们的序列变异如何与它们的微管蛋白足迹相关，反过来，这又如何解释了先前表征突变体的分子活动。随着更多高分辨率结构的出现，这种类型的评估将加快建立每个驱动蛋白的设计-功能关系的步伐。我们展示了它们的序列变异如何与它们的微管蛋白足迹相关，反过来，这又如何解释了先前表征突变体的分子活动。随着更多高分辨率结构的出现，这种类型的评估将加快建立每个驱动蛋白的设计-功能关系的步伐。