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TitleSwinging lever mechanism of myosin directly shown by time-resolved cryo-EM.
Journal, issue, pagesNature, Vol. 642, Issue 8067, Page 519-526, Year 2025
Publish dateApr 9, 2025
AuthorsDavid P Klebl / Sean N McMillan / Cristina Risi / Eva Forgacs / Betty Virok / Jennifer L Atherton / Sarah A Harris / Michele Stofella / Donald A Winkelmann / Frank Sobott / Vitold E Galkin / Peter J Knight / Stephen P Muench / Charlotte A Scarff / Howard D White /
PubMed AbstractMyosins produce force and movement in cells through interactions with F-actin. Generation of movement is thought to arise through actin-catalysed conversion of myosin from an ATP-generated primed ...Myosins produce force and movement in cells through interactions with F-actin. Generation of movement is thought to arise through actin-catalysed conversion of myosin from an ATP-generated primed (pre-powerstroke) state to a post-powerstroke state, accompanied by myosin lever swing. However, the initial, primed actomyosin state has never been observed, and the mechanism by which actin catalyses myosin ATPase activity is unclear. Here, to address these issues, we performed time-resolved cryogenic electron microscopy (cryo-EM) of a myosin-5 mutant having slow hydrolysis product release. Primed actomyosin was predominantly captured 10 ms after mixing primed myosin with F-actin, whereas post-powerstroke actomyosin predominated at 120 ms, with no abundant intermediate states detected. For detailed interpretation, cryo-EM maps were fitted with pseudo-atomic models. Small but critical changes accompany the primed motor binding to actin through its lower 50-kDa subdomain, with the actin-binding cleft open and phosphate release prohibited. Amino-terminal actin interactions with myosin promote rotation of the upper 50-kDa subdomain, closing the actin-binding cleft, and enabling phosphate release. The formation of interactions between the upper 50-kDa subdomain and actin creates the strong-binding interface needed for effective force production. The myosin-5 lever swings through 93°, predominantly along the actin axis, with little twisting. The magnitude of lever swing matches the typical step length of myosin-5 along actin. These time-resolved structures demonstrate the swinging lever mechanism, elucidate structural transitions of the power stroke, and resolve decades of conjecture on how myosins generate movement.
External linksNature / PubMed:40205053 / PubMed Central
MethodsEM (single particle)
Resolution3.9 - 4.9 Å
Structure data

19013

8r9v

EMDB-19013, PDB-8r9v:
CryoEM structure of the primed actomyosin-5a complex
Method: EM (single particle) / Resolution: 4.4 Å

19030

8rbf

EMDB-19030, PDB-8rbf:
CryoEM structure of the post-powerstroke actomyosin-5a complex
Method: EM (single particle) / Resolution: 4.2 Å

19031

8rbg

EMDB-19031, PDB-8rbg:
CryoEM structure of primed myosin-5a (ADP-Pi state)
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-50594: Rigor actomyosin-5a complex
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • mus musculus (house mouse)
  • oryctolagus cuniculus (rabbit)
KeywordsMOTOR PROTEIN / Myosin / Actin / Actomyosin / Primed actomyosin

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