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Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily

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Item Type:Review
Title:Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily
Creators Name:Daumke, O. and Praefcke, G.J.
Abstract:Dynamin superfamily proteins are multi-domain mechano-chemical GTPases which are implicated in nucleotide-dependent membrane remodeling events. A prominent feature of these proteins is their assembly-stimulated mechanism of GTP hydrolysis. The molecular basis for this reaction has been initially clarified for the dynamin-related guanylate binding protein 1 (GBP1) and involves the transient dimerization of the GTPase domains in a parallel head-to-head fashion. A catalytic arginine finger from the phosphate binding (P-) loop is repositioned towards the nucleotide of the same molecule to stabilize the transition state of GTP hydrolysis. Dynamin uses a related dimerization-dependent mechanism, but instead of the catalytic arginine, a monovalent cation is involved in catalysis. Still another variation of the GTP hydrolysis mechanism has been revealed for the dynamin-like Irga6 which bears a glycine at the corresponding position in the P-loop. Here, we highlight conserved and divergent features of GTP hydrolysis in dynamin superfamily proteins and show how nucleotide binding and hydrolysis are converted into mechano-chemical movements. We also describe models how the energy of GTP hydrolysis can be harnessed for diverse membrane remodeling events, such as membrane fission or fusion.
Keywords:Chemical Models, Dynamins, GTP-Binding Proteins, Hydrolysis, Protein Domains, Protein Multimerization, Secondary Protein Structure, Animals
Page Range:580-593
Date:August 2016
Official Publication:https://doi.org/10.1002/bip.22855
PubMed:View item in PubMed

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