High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

eLife

H Lee Sweeney¹  Sabrina Pospich²  Stefan Raunser²  Anne Houdusse³ 

[1]Department of Pharmacology and Therapeutics and the Myology Institute, University of Florida, Gainesville, United States

[2]Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany

[3]Structural Motility, Institut Curie, Centre National de la Recherche Scientifique, Paris, France

关键词: myosin;    actin;    cryo-EM;    actomyosin;    cytoskeleton;    AppNHp;    Chicken;    Human;    Rabbit;   

DOI  :  10.7554/eLife.73724

来源: eLife Sciences Publications, Ltd

【 摘 要 】

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.

【 授权许可】

CC BY