5D3Q

Dynamin 1 GTPase-BSE fusion dimer complexed with GDP

5D3Q の概要

• エントリーDOI: 10.2210/pdb5d3q/pdb
• 分子名称: Dynamin-1,Dynamin-1, GUANOSINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: hydrolase, fusion protein, gtpase, endocytosis
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm : Q05193
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78064.61

構造登録者

Anand, R.,Eschenburg, S.,Reubold, T.F. (登録日: 2015-08-06, 公開日: 2015-12-02, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)