5D3Q

Dynamin 1 GTPase-BSE fusion dimer complexed with GDP

Summary for 5D3Q

• Entry DOI: 10.2210/pdb5d3q/pdb
• Descriptor: Dynamin-1,Dynamin-1, GUANOSINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: hydrolase, fusion protein, gtpase, endocytosis
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : Q05193
• Total number of polymer chains: 2
• Total formula weight: 78064.61

Authors

Anand, R.,Eschenburg, S.,Reubold, T.F. (deposition date: 2015-08-06, release date: 2015-12-02, Last modification date: 2024-01-10)

Primary citation

Anand, R.,Eschenburg, S.,Reubold, T.F.
Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state.
Biochem.Biophys.Res.Commun., 469:76-80, 2016

PubMed Abstract: 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.

PubMed: 26612256
DOI: 10.1016/j.bbrc.2015.11.074

Experimental method

X-RAY DIFFRACTION (1.7 Å)