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11 23, 2021;10

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

Sabrina Pospich, H Lee Sweeney, Anne Houdusse, Stefan Raunser
Author Information
  1. Sabrina Pospich: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany. ORCID
  2. H Lee Sweeney: Department of Pharmacology and Therapeutics and the Myology Institute, University of Florida, Gainesville, United States. ORCID
  3. Anne Houdusse: Structural Motility, Institut Curie, Centre National de la Recherche Scientifique, Paris, France. ORCID
  4. Stefan Raunser: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany. ORCID
PMID: 34812732 DOI: 10.7554/eLife.73724

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.

Keywords

AppNHp actin actomyosin chicken cryo-EM cytoskeleton human molecular biophysics myosin rabbit structural biology

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Grants

  1. R01 DC009100/NIDCD NIH HHS

MeSH Term

Actins
Actomyosin
Animals
Biomechanical Phenomena
Chickens
Humans
Myosin Type V
Protein Binding
Rabbits

Chemicals

Actins
Actomyosin
Myosin Type V
Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't
Article has an altmetric score of 13

Word Cloud

Created with Highcharts 10.0.0myosinstructuralstructuresAppNHpmolecularmotortransitionsmechanismATPactinbindingstatescryo-EMactomyosin-Vcomplexstateprovideinsightsactomyosinundergoesseriesmajorforce-producingcycleunderlyingcouplinghydrolysispartiallyunderstoodmostlyduesparsedataactin-boundreport26high-resolutionstrong-ADPrigorpreviouslyunseenpost-rigortransitionbindsanalogrevealhighflexibilityvaluablemyosin-VuponADPreleasewellinterfaceadditionshowablespecificallyalterstructureF-actinHigh-resolutionthreenucleotideforcegenerationchickencytoskeletonhumanbiophysicsrabbitbiology

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