Crystal structure of nucleotide-free dynamin

Katja Faelber (), York Posor, Song Gao, Martin Held, Yvette Roske, Dennis Schulze, Volker Haucke, Frank Noé and Oliver Daumke ()
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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
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

Nature, 2011, vol. 477, issue 7366, 556-560

Abstract: 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.

Date: 2011
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DOI: 10.1038/nature10369

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