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


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
13 09 2021
Historique:
received: 12 12 2020
accepted: 26 08 2021
entrez: 14 9 2021
pubmed: 15 9 2021
medline: 21 10 2021
Statut: epublish

Résumé

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.

Identifiants

pubmed: 34518553
doi: 10.1038/s41467-021-25741-x
pii: 10.1038/s41467-021-25741-x
pmc: PMC8437954
doi:

Substances chimiques

Guanosine Triphosphate 86-01-1
Dynamin I EC 3.5.1.50
GTP Phosphohydrolases EC 3.6.1.-

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

5393

Subventions

Organisme : NIGMS NIH HHS
ID : P50 GM082251
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM085043
Pays : United States
Organisme : Wellcome Trust
ID : 206422/Z/17/Z
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : P50 AI150481
Pays : United States
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/S003339/1
Pays : United Kingdom
Organisme : Medical Research Council
Pays : United Kingdom

Informations de copyright

© 2021. The Author(s).

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Auteurs

Jiwei Liu (J)

Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.

Frances Joan D Alvarez (FJD)

Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15260, USA.

Daniel K Clare (DK)

Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK.

Jeffrey K Noel (JK)

Electric Ant Lab, Amsterdam, The Netherlands.

Peijun Zhang (P)

Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK. peijun.zhang@strubi.ox.ac.uk.
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15260, USA. peijun.zhang@strubi.ox.ac.uk.
Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. peijun.zhang@strubi.ox.ac.uk.

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