Crystal structure of nucleotide-free dynamin

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 cry...

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Veröffentlicht in:	Nature (London) 2011-09, Vol.477 (7366), p.556-560
Hauptverfasser:	Faelber, Katja, Posor, York, Gao, Song, Held, Martin, Roske, Yvette, Schulze, Dennis, Haucke, Volker, Noé, Frank, Daumke, Oliver
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/535 631/45/612/1237 631/57/2272 Crystal structure Crystallography, X-Ray Crystals Dynamin I - chemistry Dynamin I - metabolism Dynamin II - genetics Dynamin II - metabolism GTP Phosphohydrolases - chemistry GTP Phosphohydrolases - metabolism Guanosine Triphosphate - metabolism HeLa Cells Humanities and Social Sciences Humans Hydrolysis Lipids Models, Molecular Molecular Dynamics Simulation multidisciplinary Mutation Nucleotides Protein Binding Protein Structure, Tertiary Proteins Science Science (multidisciplinary) Signal Transduction Transferrin - metabolism
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