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CryoEM structure of the super-constricted two-start dynamin 1 filament

Author

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  • Jiwei Liu

    (University of Oxford)

  • Frances Joan D. Alvarez

    (University of Pittsburgh School of Medicine)

  • Daniel K. Clare

    (Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus)

  • Jeffrey K. Noel

    (Electric Ant Lab)

  • Peijun Zhang

    (University of Oxford
    University of Pittsburgh School of Medicine
    Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus)

Abstract

Dynamin belongs to the large GTPase superfamily, and mediates the fission of vesicles during endocytosis. Dynamin molecules are recruited to the neck of budding vesicles to assemble into a helical collar and to constrict the underlying membrane. Two helical forms were observed: the one-start helix in the constricted state and the two-start helix in the super-constricted state. Here we report the cryoEM structure of a super-constricted two-start dynamin 1 filament at 3.74 Å resolution. The two strands are joined by the conserved GTPase dimeric interface. In comparison with the one-start structure, a rotation around Hinge 1 is observed, essential for communicating the chemical power of the GTPase domain and the mechanical force of the Stalk and PH domain onto the underlying membrane. The Stalk interfaces are well conserved and serve as fulcrums for adapting to changing curvatures. Relative to one-start, small rotations per interface accumulate to bring a drastic change in the helical pitch. Elasticity theory rationalizes the diversity of dynamin helical symmetries and suggests corresponding functional significance.

Suggested Citation

  • Jiwei Liu & Frances Joan D. Alvarez & Daniel K. Clare & Jeffrey K. Noel & Peijun Zhang, 2021. "CryoEM structure of the super-constricted two-start dynamin 1 filament," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25741-x
    DOI: 10.1038/s41467-021-25741-x
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