7PM1

Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, young JASP-stabilized F-actin, class 2)

Summary for 7PM1

• Entry DOI: 10.2210/pdb7pm1/pdb
• Related: 7PLY 7PM0 7PM2
• EMDB information: 13509
• Descriptor: Myosin light chain 6B, Unconventional myosin-Va, Actin, alpha skeletal muscle, ... (7 entities in total)
• Functional Keywords: motor protein, myosin, cytoskeleton, f-actin, jasplakinolide
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 151820.35

Authors

Pospich, S.,Sweeney, H.L.,Houdusse, A.,Raunser, S. (deposition date: 2021-09-01, release date: 2021-12-22)

Primary citation

Pospich, S.,Sweeney, H.L.,Houdusse, A.,Raunser, S.
High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.
Elife, 10:-, 2021

PubMed Abstract: 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.

PubMed: 34812732
DOI: 10.7554/eLife.73724

Experimental method

ELECTRON MICROSCOPY (3.5 Å)