1JX2

CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION

1JX2 の概要

• エントリーDOI: 10.2210/pdb1jx2/pdb
• 関連するPDBエントリー: 1JWY
• 分子名称: Myosin-2 heavy chain,Dynamin-A, beta-D-glucopyranose, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: dynamin, gtpase, myosin, fusion-protein, dictyostelium, hydrolase
• 由来する生物種: Dictyostelium discoideum (Slime mold); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 125205.19

構造登録者

Niemann, H.H.,Knetsch, M.L.W.,Scherer, A.,Manstein, D.J.,Kull, F.J. (登録日: 2001-09-05, 公開日: 2001-11-07, 最終更新日: 2024-10-30)

主引用文献

Niemann, H.H.,Knetsch, M.L.,Scherer, A.,Manstein, D.J.,Kull, F.J.
Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.
EMBO J., 20:5813-5821, 2001

PubMed Abstract: Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 A crystal structure of the nucleotide-free and GDP-bound GTPase domain of Dictyostelium discoideum dynamin A. The GTPase domain is the most highly conserved region among dynamins. The globular structure contains the G-protein core fold, which is extended from a six-stranded beta-sheet to an eight-stranded one by a 55 amino acid insertion. This topologically unique insertion distinguishes dynamins from other subfamilies of GTP-binding proteins. An additional N-terminal helix interacts with the C-terminal helix of the GTPase domain, forming a hydrophobic groove, which could be occupied by C-terminal parts of dynamin not present in our construct. The lack of major conformational changes between the nucleotide-free and the GDP-bound state suggests that mechanochemical rearrangements in dynamin occur during GTP binding, GTP hydrolysis or phosphate release and are not linked to loss of GDP.

PubMed: 11689422
DOI: 10.1093/emboj/20.21.5813

実験手法

X-RAY DIFFRACTION (2.3 Å)