Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity

Simple item page
dc.citation.articleNumbere1005035en_US
dc.citation.issueNumber8en_US
dc.citation.journalTitlePLoS Computational Biologyen_US
dc.citation.volumeNumber12en_US
dc.contributor.authorJana, Bimanen_US
dc.contributor.authorOnuchic, José N.en_US
dc.contributor.orgCenter for Theoretical Biological Physicsen_US
dc.date.accessioned2016-09-30T20:52:22Zen_US
dc.date.available2016-09-30T20:52:22Zen_US
dc.date.issued2016en_US
dc.description.abstractA structure-based model of myosin motor is built in the same spirit of our early work for kinesin-1 and Ncd towards physical understanding of its mechanochemical cycle. We find a structural adaptation of the motor head domain in post-powerstroke state that signals faster ADP release from it compared to the same from the motor head in the pre-powerstroke state. For dimeric myosin, an additional forward strain on the trailing head, originating from the postponed powerstroke state of the leading head in the waiting state of myosin, further increases the rate of ADP release. This coordination between the two heads is the essence of the processivity of the cycle. Our model provides a structural description of the powerstroke step of the cycle as an allosteric transition of the converter domain in response to the Pirelease. Additionally, the variation in structural elements peripheral to catalytic motor domain is the deciding factor behind diverse directionalities of myosin motors (myosin V & VI). Finally, we observe that there are general rules for functional molecular motors across the different families. Allosteric structural adaptation of the catalytic motor head in different nucleotide states is crucial for mechanochemistry. Strain-mediated coordination between motor heads is essential for processivity and the variation of peripheral structural elements is essential for their diverse functionalities.en_US
dc.identifier.citationJana, Biman and Onuchic, José N.. "Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity." <i>PLoS Computational Biology,</i> 12, no. 8 (2016) Public Library of Science: http://dx.doi.org/10.1371/journal.pcbi.1005035.en_US
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pcbi.1005035en_US
dc.identifier.urihttps://hdl.handle.net/1911/91624en_US
dc.language.isoengen_US
dc.publisherPublic Library of Scienceen_US
dc.rightsThis is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.titleStrain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activityen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
journal.pcbi.1005035.pdf
Size:
4.24 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Faculty Publications