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Crystal structure of nucleotide-free dynamin

Author

Listed:
  • Katja Faelber

    (Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany)

  • York Posor

    (Institute for Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany)

  • Song Gao

    (Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany
    Institute for Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany)

  • Martin Held

    (Institute for Mathematics, Freie Universität Berlin, Arnimallee 6, 14195 Berlin, Germany)

  • Yvette Roske

    (Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany)

  • Dennis Schulze

    (Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany)

  • Volker Haucke

    (Institute for Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany)

  • Frank Noé

    (Institute for Mathematics, Freie Universität Berlin, Arnimallee 6, 14195 Berlin, Germany)

  • Oliver Daumke

    (Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany
    Institute for Medical Physics and Biophysics, Charité, Ziegelstraße 5-9, 10117 Berlin, Germany)

Abstract

Dynamin is a mechanochemical GTPase that oligomerizes around the neck of clathrin-coated pits and catalyses vesicle scission in a GTP-hydrolysis-dependent manner. The molecular details of oligomerization and the mechanism of the mechanochemical coupling are currently unknown. Here we present the crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. Dynamin 1 oligomerized in the crystals via the stalks, which assemble in a criss-cross fashion. The stalks further interact via conserved surfaces with the pleckstrin homology domain and the bundle signalling element of the neighbouring dynamin molecule. This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.

Suggested Citation

  • Katja Faelber & York Posor & Song Gao & Martin Held & Yvette Roske & Dennis Schulze & Volker Haucke & Frank Noé & Oliver Daumke, 2011. "Crystal structure of nucleotide-free dynamin," Nature, Nature, vol. 477(7366), pages 556-560, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7366:d:10.1038_nature10369
    DOI: 10.1038/nature10369
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    Cited by:

    1. Kristy Rochon & Brianna L. Bauer & Nathaniel A. Roethler & Yuli Buckley & Chih-Chia Su & Wei Huang & Rajesh Ramachandran & Maria S. K. Stoll & Edward W. Yu & Derek J. Taylor & Jason A. Mears, 2024. "Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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