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Mechanochemistry of the kinesin-1 ATPase
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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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Official URL: http://dx.doi.org/10.1002/bip.22862
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 | ||||||||||
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Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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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: |
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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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