Cross, R. A. (2016) Mechanochemistry of the kinesin-1 ATPase. Biopolymers, 105 (8). pp. 476-482. doi:10.1002/bip.22862 ISSN 1097-0282.

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Abstract

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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology
Divisions:	Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH):	Kinesiology, Kinesin, Adenosine triphosphatase, Mechanical chemistry
Journal or Publication Title:	Biopolymers
Publisher:	John Wiley & Sons, Inc.,
ISSN:	1097-0282
Official Date:	August 2016
Dates:	Date Event August 2016 Published 20 May 2016 Available 27 April 2016 Available 17 April 2016 Accepted
Volume:	105
Number:	8
Page Range:	pp. 476-482
DOI:	10.1002/bip.22862
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Date of first compliant deposit:	1 June 2016
Date of first compliant Open Access:	3 June 2016

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