4PHG

Crystal structure of Ypt7 covalently modified with GTP

4PHG の概要

• エントリーDOI: 10.2210/pdb4phg/pdb
• 関連するPDBエントリー: 4PHF 4PHH
• 分子名称: GTP-binding protein YPT7, MAGNESIUM ION, N-[3-(propanoylamino)propyl]guanosine 5'-(tetrahydrogen triphosphate), ... (5 entities in total)
• 機能のキーワード: ypt7, acryl-nucleotides, agtp, covalent, endocytosis, exocytosis
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21226.34

構造登録者

Koch, D.,Wiegandt, D.,Vieweg, S.,Hofmann, F.,Wu, Y.,Itzen, A.,Mueller, M.P.,Goody, R.S. (登録日: 2014-05-06, 公開日: 2014-05-28, 最終更新日: 2024-10-16)

主引用文献

Wiegandt, D.,Vieweg, S.,Hofmann, F.,Koch, D.,Li, F.,Wu, Y.W.,Itzen, A.,Muller, M.P.,Goody, R.S.
Locking GTPases covalently in their functional states.
Nat Commun, 6:7773-7773, 2015

PubMed Abstract: GTPases act as key regulators of many cellular processes by switching between active (GTP-bound) and inactive (GDP-bound) states. In many cases, understanding their mode of action has been aided by artificially stabilizing one of these states either by designing mutant proteins or by complexation with non-hydrolysable GTP analogues. Because of inherent disadvantages in these approaches, we have developed acryl-bearing GTP and GDP derivatives that can be covalently linked with strategically placed cysteines within the GTPase of interest. Binding studies with GTPase-interacting proteins and X-ray crystallography analysis demonstrate that the molecular properties of the covalent GTPase-acryl-nucleotide adducts are a faithful reflection of those of the corresponding native states and are advantageously permanently locked in a defined nucleotide (that is active or inactive) state. In a first application, in vivo experiments using covalently locked Rab5 variants provide new insights into the mechanism of correct intracellular localization of Rab proteins.

PubMed: 26178622
DOI: 10.1038/ncomms8773

実験手法

X-RAY DIFFRACTION (1.9 Å)