Format

Send to

Choose Destination
Structure. 2010 Mar 14;18(4):458-70. doi: 10.1016/j.str.2010.01.014.

Pi release from myosin: a simulation analysis of possible pathways.

Author information

1
Laboratoire de Chimie Biophysique, ISIS, Université de Strasbourg, 67000 Strasbourg, France. mcecchini@isis.u-strasbg.fr

Abstract

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.

Comment in

PMID:
20399183
PMCID:
PMC2858069
DOI:
10.1016/j.str.2010.01.014
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center