7pmg
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Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state (AppNHp, central 1er, class 3)
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Structural highlights
FunctionMYO5A_CHICK Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity). Publication Abstract from PubMedThe 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 is 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. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.,Pospich S, Sweeney HL, Houdusse A, Raunser S Elife. 2021 Nov 23;10. pii: 73724. doi: 10.7554/eLife.73724. PMID:34812732[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 08:26, 4 March 2026.