Crystal structure of nucleotide-free dynamin

Item Type:	Article
Title:	Crystal structure of nucleotide-free dynamin
Creators Name:	Faelber, K. and Posor, Y. and Gao, S. and Held, M. and Roske, Y. and Schulze, D. and Haucke, V. and Noe, F. and Daumke, O.
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.
Keywords:	Biochemistry, Biophysics, Molecular Biology, Structural Biology
Source:	Nature
ISSN:	0028-0836
Publisher:	Nature Publishing Group
Volume:	477
Number:	7366
Page Range:	556-560
Date:	29 September 2011
Official Publication:	https://doi.org/10.1038/nature10369
PubMed:	View item in PubMed

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