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TitleExploiting cryo-EM structures of actomyosin-5a to reveal the physical properties of its lever.
Journal, issue, pagesStructure, Vol. 32, Issue 12, Page 2316-22324.e6, Year 2024
Publish dateDec 5, 2024
AuthorsMolly S C Gravett / David P Klebl / Oliver G Harlen / Daniel J Read / Stephen P Muench / Sarah A Harris / Michelle Peckham /
PubMed AbstractMyosin 5a (Myo5a) is a dimeric processive motor protein that transports cellular cargos along filamentous actin (F-actin). Its long lever is responsible for its large power-stroke, step size, and ...Myosin 5a (Myo5a) is a dimeric processive motor protein that transports cellular cargos along filamentous actin (F-actin). Its long lever is responsible for its large power-stroke, step size, and load-bearing ability. Little is known about the levers' structure and physical properties, and how they contribute to walking mechanics. Using cryoelectron microscopy (cryo-EM) and molecular dynamics (MD) simulations, we resolved the structure of monomeric Myo5a, comprising the motor domain and full-length lever, bound to F-actin. The range of its lever conformations revealed its physical properties, how stiffness varies along its length and predicts a large, 35 nm, working stroke. Thus, the newly released trail head in a dimeric Myo5a would only need to perform a small diffusive search for its new binding site on F-actin, and stress would only be generated across the dimer once phosphate is released from the lead head, revealing new insight into the walking behavior of Myo5a.
External linksStructure / PubMed:39454567
MethodsEM (single particle)
Resolution4.2 - 10.7 Å
Structure data

EMDB-16846: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class A)
Method: EM (single particle) / Resolution: 8.6 Å

EMDB-16848: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class B)
Method: EM (single particle) / Resolution: 8.1 Å

EMDB-16849: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class C)
Method: EM (single particle) / Resolution: 7.7 Å

16850

8of8

EMDB-16850: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class D)
PDB-8of8: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-16851: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class E)
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-16852: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class G)
Method: EM (single particle) / Resolution: 10.7 Å

EMDB-16853: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class F)
Method: EM (single particle) / Resolution: 8.1 Å

EMDB-16854: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class H)
Method: EM (single particle) / Resolution: 8.2 Å

EMDB-16855: Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free, class I)
Method: EM (single particle) / Resolution: 9.7 Å

EMDB-16856: Cryo-EM structure of actomyosin-5a-S1(nucleotide free, motor + 2IQ)
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • oryctolagus cuniculus (rabbit)
  • mus musculus (house mouse)
KeywordsMOTOR PROTEIN / myosin / cytoskeletal motor / myosin-va / myo5a / myosin-5a / S1 / rigor / nucleotide free / apo / lever / 6IQ / actomyosin / actomyosin-5a / actin / actomyosin-va / actin bound

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