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: | , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
March 14, 2016
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| 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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| 520 | |a 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. | ||
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