Crystal structure of nucleotide-free dynamin

K Faelber, Y Posor, S Gao, M Held, Y Roske… - Nature, 2011 - nature.com
K Faelber, Y Posor, S Gao, M Held, Y Roske, D Schulze, V Haucke, F Noé, O Daumke
Nature, 2011nature.com
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 …
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.
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