Structural highlights
Function
[DYN1_HUMAN] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
Publication Abstract from PubMed
Dynamin is the prototype of a family of large multi-domain GTPases. The 100 kDa protein is a key player in clathrin-mediated endocytosis, where it cleaves off vesicles from membranes using the energy from GTP hydrolysis. We have solved the high resolution crystal structure of a fusion protein of the GTPase domain and the bundle signalling element (BSE) of dynamin 1 liganded with GDP. The structure provides a hitherto missing snapshot of the GDP state of the hydrolytic cycle of dynamin and reveals how the switch I region moves away from the active site after GTP hydrolysis and release of inorganic phosphate. Comparing our structure of the GDP state with the known structures of the GTP state, the transition state and the nucleotide-free state of dynamin 1 we describe the structural changes through the hydrolytic cycle.
Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state.,Anand R, Eschenburg S, Reubold TF Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Anand R, Eschenburg S, Reubold TF. Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state. Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256 doi:http://dx.doi.org/10.1016/j.bbrc.2015.11.074
