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• W1970851569 abstract "Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin's basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-).The structure reveals dynamin's catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase-GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission." @default.
• W1970851569 created "2016-06-24" @default.
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• W1970851569 date "2010-04-28" @default.
• W1970851569 modified "2023-10-16" @default.
• W1970851569 title "G domain dimerization controls dynamin's assembly-stimulated GTPase activity" @default.
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• W1970851569 doi "https://doi.org/10.1038/nature09032" @default.
• W1970851569 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2879890" @default.
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