TY - JOUR TI - High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism AU - Pospich, Sabrina AU - Sweeney, H Lee AU - Houdusse, Anne AU - Raunser, Stefan A2 - Reck-Peterson, Samara L A2 - Faraldo-Gómez, José D A2 - Ostap, E Michael VL - 10 PY - 2021 DA - 2021/11/23 SP - e73724 C1 - eLife 2021;10:e73724 DO - 10.7554/eLife.73724 UR - https://doi.org/10.7554/eLife.73724 AB - The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin. KW - myosin KW - actin KW - cryo-EM KW - actomyosin KW - cytoskeleton KW - AppNHp JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -