Review: Mechanochemistry of the kinesin-1 ATPase.
Review: Mechanochemistry of the kinesin-1 ATPase.
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评论：运动蛋白-1 ATPase的机械化学。
DOI：
10.1002/bip.22862
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发表时间：
2016-08
期刊：
影响因子：
2.9
通讯作者：
Cross RA
中科院分区：
文献类型：
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作者：
Cross RA
驱动蛋白是一种可以做机械功的P环NTPases。像小G蛋白一样，驱动蛋白执行活性位点构象变化的程序，从NTP底物上切割末端磷酸盐。但与小G蛋白不同，驱动蛋白可以放大和利用这些构象变化来施加力。在这篇简短的综述中，我总结了目前关于驱动蛋白活性位点如何工作的想法，并概述了活性位点化学如何与驱动蛋白运动域的大规模结构周期相耦合。主要集中在驱动蛋白-1，研究最好的驱动蛋白，我讨论了驱动蛋白的活性位点开关机制之间的三个不同的状态，如何对接的颈连接器稳定这些状态中的两个，以及如何张力敏感和位置敏感的颈连接器对接可能会调节ATP周转的水解步骤和产品ADP在活性位点的捕获。© 2016 Wiley Periodicals，Inc. Biopolymers 105：476-482，2016.
Kinesins are P‐loop NTPases that can do mechanical work. Like small G‐proteins, to which they are related, kinesins execute a program of active site conformational changes that cleaves the terminal phosphate from an NTP substrate. But unlike small G‐proteins, kinesins can amplify and harness these conformational changes in order to exert force. In this short review I summarize current ideas about how the kinesin active site works and outline how the active site chemistry is coupled to the larger‐scale structural cycle of the kinesin motor domain. Focusing largely on kinesin‐1, the best‐studied kinesin, I discuss how the active site switch machinery of kinesin cycles between three distinct states, how docking of the neck linker stabilizes two of these states, and how tension‐sensitive and position‐sensitive neck linker docking may modulate both the hydrolysis step of ATP turnover and the trapping of product ADP in the active site. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 476–482, 2016.