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Structural basis of oligomerization in the stalk region of dynamin-like MxA

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  • Song Gao

    (Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany
    Institute for Chemistry and Biochemistry, Free University Berlin, Takustrasse 3, 14195 Berlin, Germany)

  • Alexander von der Malsburg

    (Institute for Medical Microbiology and Hygiene, University of Freiburg, Hermann-Herder-Strasse 11, 79104 Freiburg, Germany)

  • Susann Paeschke

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

  • Joachim Behlke

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

  • Otto Haller

    (Institute for Medical Microbiology and Hygiene, University of Freiburg, Hermann-Herder-Strasse 11, 79104 Freiburg, Germany)

  • Georg Kochs

    (Institute for Medical Microbiology and Hygiene, University of Freiburg, Hermann-Herder-Strasse 11, 79104 Freiburg, Germany)

  • Oliver Daumke

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

Abstract

Crystal structure of dynamin-like MxA The GTPase dynamin catalyses the scission of clathrin-coated pits at the plasma membrane, but the mechanisms of dynamin-mediated membrane fission remain poorly understood. Here, Gao et al. study a dynamin-like GTPase called MxA, which plays an important role in innate immune responses. They present the crystal structure of the stalk region of MxA that is composed of the middle domain and the GTPase effector domain (GED). A structural model of MxA oligomerization and stimulated GTP hydrolysis is presented, which has functional implications for all members of the dynamin family.

Suggested Citation

  • Song Gao & Alexander von der Malsburg & Susann Paeschke & Joachim Behlke & Otto Haller & Georg Kochs & Oliver Daumke, 2010. "Structural basis of oligomerization in the stalk region of dynamin-like MxA," Nature, Nature, vol. 465(7297), pages 502-506, May.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7297:d:10.1038_nature08972
    DOI: 10.1038/nature08972
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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.
    2. Lucas Gewehr & Benedikt Junglas & Ruven Jilly & Johannes Franz & Wenyu Eva Zhu & Tobias Weidner & Mischa Bonn & Carsten Sachse & Dirk Schneider, 2023. "SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Ruth E. Drury & Susana Camara & Irina Chelysheva & Sagida Bibi & Katherine Sanders & Salle Felle & Katherine Emary & Daniel Phillips & Merryn Voysey & Daniela M. Ferreira & Paul Klenerman & Sarah C. G, 2024. "Multi-omics analysis reveals COVID-19 vaccine induced attenuation of inflammatory responses during breakthrough disease," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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