2X2F

Dynamin 1 GTPase dimer, short axis form

2X2F の概要

• エントリーDOI: 10.2210/pdb2x2f/pdb
• 関連するPDBエントリー: 1DYN 2DYN 2X2E
• 分子名称: DYNAMIN-1, GUANOSINE-5'-DIPHOSPHATE, TETRAFLUOROALUMINATE ION, ... (6 entities in total)
• 機能のキーワード: nitration, hydrolase, membrane fission, nucleotide-binding, endocytosis, motor protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80715.18

構造登録者

Chappie, J.S.,Acharya, S.,Leonard, M.,Schmid, S.L.,Dyda, F. (登録日: 2010-01-13, 公開日: 2010-04-28, 最終更新日: 2024-11-20)

主引用文献

Chappie, J.S.,Acharya, S.,Leonard, M.,Schmid, S.L.,Dyda, F.
G Domain Dimerization Controls Dynamin'S Assembly-Stimulated Gtpase Activity.
Nature, 465:435-, 2010

PubMed Abstract: Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin's basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-).The structure reveals dynamin's catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase-GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission.

PubMed: 20428113
DOI: 10.1038/NATURE09032

実験手法

X-RAY DIFFRACTION (2 Å)