Journal
ELIFE
Volume 10, Issue -, Pages -Publisher
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.73724
Keywords
myosin; actin; cryo-EM; actomyosin; cytoskeleton; AppNHp; Chicken; Human; Rabbit
Categories
Funding
- Max-Planck-Gesellschaft
- Horizon 2020 [ERC-2019-SyG 856118]
- Agence Nationale de la Recherche [ANR-17-CE11-0029-01]
- National Institutes of Health [R01-DC009100]
- Centre National de la Recherche Scientifique
- Studienstiftung des Deutschen Volkes
- Agence Nationale de la Recherche (ANR) [ANR-17-CE11-0029] Funding Source: Agence Nationale de la Recherche (ANR)
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This study reports the structural transitions of the molecular motor myosin during its force-producing motor cycle, providing valuable insights into the high-resolution structures of myosin-V in different states.
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.
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