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

Song Gao, Alexander von der Malsburg, Susann Paeschke, Joachim Behlke, Otto Haller, Georg Kochs and Oliver Daumke ()
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Song Gao: Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 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

Nature, 2010, vol. 465, issue 7297, 502-506

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.

Date: 2010
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DOI: 10.1038/nature08972

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