ArticlePLoS computational biology2016
Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity.
Article in PLoS computational biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Unraveling Mutation-Induced Protein Communication Pathways in the Actomyosin Complex: Insights from Comprehensive Metadynamics Simulations.The journal of physical chemistry. B · 2025Article
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
- A VDAC1-mediated NEET protein chain transfers [2Fe-2S] clusters between the mitochondria and the cytosol and impacts mitochondrial dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanistic basis of propofol-induced disruption of kinesin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- Structural consequences of hereditary spastic paraplegia disease-related mutations in kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 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 Pi release. 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.
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