Review: Mechanochemistry of the kinesin-1 ATPase.
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.
Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, CV4 7AL, UK.
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D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D020134:Catalytic Domain; D006801:Humans; D006868:Hydrolysis; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary
D000255:Adenosine Triphosphate; D016547:Kinesins
ATPase; kinesin; mechanochemistry