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Force-producing ADP state of myosin bound to actin

Molecular motors produce force when they interact with their cellular tracks. For myosin motors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to actin. We have generated an 8-Å cryoEM reconstruction of this state for myosin V and used molecular dynami...

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Main Authors: Wulf, Sarah Elise Freyja (Author) , Ropars, Virginie (Author) , Fujita-Becker, Setsuko (Author) , Oster, Marco (Author) , Hofhaus, Götz (Author) , Trabuco, Leonardo G. (Author) , Pylypenko, Olena (Author) , Sweeney, H. Lee (Author) , Houdusse, Anne M. (Author) , Schröder, Rasmus R. (Author)
Format: Article (Journal)
Language:English
Published: March 14, 2016
In: Proceedings of the National Academy of Sciences of the United States of America
Year: 2016, Volume: 113, Issue: 13, Pages: E1844-E1852
ISSN:1091-6490
DOI:10.1073/pnas.1516598113
Online Access:Verlag, Volltext: https://doi.org/10.1073/pnas.1516598113
Verlag, Volltext: https://www.pnas.org/content/113/13/E1844
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Author Notes:Sarah F. Wulf, Virginie Ropars, Setsuko Fujita-Becker, Marco Oster, Goetz Hofhaus, Leonardo G. Trabuco, Olena Pylypenko, H. Lee Sweeney, Anne M. Houdusse, and Rasmus R. Schröder
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Summary:Molecular motors produce force when they interact with their cellular tracks. For myosin motors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to actin. We have generated an 8-Å cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for model building. We compare this state to the subsequent state on actin (Rigor). The ADP-bound structure reveals that the actin-binding cleft is closed, even though MgADP is tightly bound. This state is accomplished by a previously unseen conformation of the β-sheet underlying the nucleotide pocket. The transition from the force-generating ADP state to Rigor requires a 9.5° rotation of the myosin lever arm, coupled to a β-sheet rearrangement. Thus, the structure reveals the detailed rearrangements underlying myosin force generation as well as the basis of strain-dependent ADP release that is essential for processive myosins, such as myosin V.
Item Description:Gesehen am 18.02.2020
Physical Description:Online Resource
ISSN:1091-6490
DOI:10.1073/pnas.1516598113

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