Pi release from myosin: a simulation analysis of possible pathways

Cecchini, Marco; Alexeev, Yuri; Karplus, Martin (2010). Pi release from myosin: a simulation analysis of possible pathways. Structure, 18(4), pp. 458-70. Cambridge, Mass.: Cell Press 10.1016/j.str.2010.01.014

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The release of phosphate (Pi) is an important element in actomyosin function and has been shown to be accelerated by the binding of myosin to actin. To provide information about the structural elements important for Pi release, possible escape pathways from various isolated myosin II structures have been determined by molecular dynamics simulations designed for studying such slow processes. The residues forming the pathways were identified and their role was evaluated by mutant simulations. Pi release is slow in the pre-powerstroke structure, an important element in preventing the powerstroke prior to actin binding, and is much more rapid for Pi modeled into the post-rigor and rigor-like structures. The previously proposed backdoor route is dominant in the pre-powerstroke and post-rigor states, whereas a different path is most important in the rigor-like state. This finding suggests a mechanism for the actin-activated acceleration of Pi release.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Dermatology, Urology, Rheumatology, Nephrology, Osteoporosis (DURN) > Clinic of Urology

UniBE Contributor:

Cecchini, Marco Giovanni

ISSN:

0969-2126

Publisher:

Cell Press

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:10

Last Modified:

04 May 2014 23:05

Publisher DOI:

10.1016/j.str.2010.01.014

PubMed ID:

20399183

Web of Science ID:

000276781500007

URI:

https://boris.unibe.ch/id/eprint/1252 (FactScience: 202406)

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