1S9D

ARF1[DELTA 1-17]-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN

「1R8R」から置き換えられました

1S9D の概要

• エントリーDOI: 10.2210/pdb1s9d/pdb
• 関連するPDBエントリー: 1PBV 1R8M 1R8Q 1R8S
• 分子名称: ADP-Ribosylation Factor 1, Arno, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: protein transport/exchange factor, protein transport-exchange factor complex
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Golgi apparatus: P84080; Cell membrane ; Peripheral membrane protein : Q99418
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43085.07

構造登録者

Renault, L.,Guibert, B.,Cherfils, J. (登録日: 2004-02-04, 公開日: 2004-02-10, 最終更新日: 2024-10-30)

主引用文献

Renault, L.,Guibert, B.,Cherfils, J.
Structural Snapshots of the Mechanism and Inhibition of a Guanine Nucleotide Exchange Factor
Nature, 426:525-530, 2003

PubMed Abstract: Small GTP-binding (G) proteins are activated by GDP/GTP nucleotide exchange stimulated by guanine nucleotide exchange factors (GEFs). Nucleotide dissociation from small G protein-GEF complexes involves transient GDP-bound intermediates whose structures have never been described. In the case of Arf proteins, small G proteins that regulate membrane traffic in eukaryotic cells, such intermediates can be trapped either by the natural inhibitor brefeldin A or by charge reversal at the catalytic glutamate of the Sec7 domain of their GEFs. Here we report the crystal structures of these intermediates that show that membrane recruitment of Arf and nucleotide dissociation are separate reactions stimulated by Sec7. The reactions proceed through sequential rotations of the Arf.GDP core towards the Sec7 catalytic site, and are blocked by interfacial binding of brefeldin A and unproductive stabilization of GDP by charge reversal. The structural characteristics of the reaction and its modes of inhibition reveal unexplored ways in which to inhibit the activation of small G proteins.

PubMed: 14654833
DOI: 10.1038/nature02197

実験手法

X-RAY DIFFRACTION (1.8 Å)