Allosteric Communication in Myosin V: From Small Conformational Changes to Large Directed Movements

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Allosteric Communication in Myosin V: From Small Conformational Changes to Large Directed Movements

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dc.contributor.author Houdusse, A.
dc.contributor.author Cecchini, M.
dc.contributor.author Karplus, Martin
dc.date.accessioned 2009-02-25T02:39:29Z
dc.date.issued 2008
dc.identifier.citation Cecchini, M., A. Houdusse A, and M. Karplus. 2008. Allosteric communication in myosin V: from small conformational changes to large directed movements. PLoS Computational Biolology 4(8): e1000129. en
dc.identifier.issn 1553-7358 en
dc.identifier.issn 1553-734X en
dc.identifier.uri http://nrs.harvard.edu/urn-3:HUL.InstRepos:2633259
dc.description.abstract The rigor to post-rigor transition in myosin, a consequence of ATP binding, plays an essential role in the Lymn–Taylor functional cycle because it results in the dissociation of the actomyosin complex after the powerstroke. On the basis of the X-ray structures of myosin V, we have developed a new normal mode superposition model for the transition path between the two states. Rigid-body motions of the various subdomains and specific residues at the subdomain interfaces are key elements in the transition. The allosteric communication between the nucleotide binding site and the U50/L50 cleft is shown to result from local changes due to ATP binding, which induce large amplitude motions that are encoded in the structure of the protein. The triggering event is the change in the interaction of switch I and the P-loop, which is stabilized by ATP binding. The motion of switch I, which is a relatively rigid element of the U50 subdomain, leads directly to a partial opening of the U50/L50 cleft; the latter is expected to weaken the binding of myosin to actin. The calculated transition path demonstrates the nature of the subdomain coupling and offers an explanation for the mutual exclusion of ATP and actin binding. The mechanism of the uncoupling of the converter from the motor head, an essential part of the transition, is elucidated. The origin of the partial untwisting of the central ?-sheet in the rigor to post-rigor transition is described. en
dc.description.sponsorship Chemistry and Chemical Biology en
dc.language.iso en_US en
dc.publisher Public Library of Science en
dc.relation.isversionof http://dx.doi.org/10.1371/journal.pcbi.1000129 en
dash.license LAA
dc.subject protein chemistry en
dc.subject biochemistry: theory and simulation en
dc.subject macromolecular assemblies and machines en
dc.subject membrane proteins and energy transduction en
dc.subject biochemistry
dc.title Allosteric Communication in Myosin V: From Small Conformational Changes to Large Directed Movements en
dc.type Journal Article
dc.description.version Version of Record
dc.relation.journal PLoS Computational Biology en
dash.depositing.author Karplus, Martin

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  • FAS Scholarly Articles [7106]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University

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