IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v465y2010i7297d10.1038_nature08972.html
   My bibliography  Save this article

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

Author

Listed:
  • 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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08972
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature08972?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. 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.
    2. 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.
    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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:465:y:2010:i:7297:d:10.1038_nature08972. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.