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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 |
| Source: | Biopolymers |
| ISSN: | 0006-3525 |
| Publisher: | Wiley |
| Volume: | 105 |
| Number: | 8 |
| 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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