2E7S

Crystal structure of the yeast Sec2p GEF domain

2E7S の概要

• エントリーDOI: 10.2210/pdb2e7s/pdb
• 分子名称: Rab guanine nucleotide exchange factor SEC2 (2 entities in total)
• 機能のキーワード: coiled coil, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Bud neck: P17065
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 315610.28

構造登録者

Fukai, S.,Sato, Y.,Nureki, O. (登録日: 2007-01-12, 公開日: 2007-02-27, 最終更新日: 2024-10-30)

主引用文献

Sato, Y.,Shirakawa, R.,Horiuchi, H.,Dohmae, N.,Fukai, S.,Nureki, O.
Asymmetric Coiled-Coil Structure with Guanine Nucleotide Exchange Activity
Structure, 15:245-252, 2007

PubMed Abstract: Vesicular traffic during exocytosis is regulated by Rab GTPase, Sec4p in yeast, which is activated by a guanine nucleotide exchange factor (GEF) called Sec2p. The GEF activity is localized in the N-terminal 160 residues of Sec2p, which lacks sequence similarity with any other GEFs with known structures, and thereby the guanine nucleotide exchange mechanism by Sec2p remains unknown. Here, we report the crystal structure of the Sec2p GEF domain at 3.0 A resolution. The structure unexpectedly consists of a homodimeric, parallel coiled coil that extends over 180 A. Pull-down and guanine nucleotide exchange analyses on a series of deletion and point mutants of Sec2p unveiled the catalytic residues for its GEF activity as well as the Sec4p binding site, thus presenting a nucleotide exchange mechanism by a simple coiled coil. The present functional analyses allow us to build the Sec2p:Sec4p complex model, which explains the specificity for Rab GTPases by their respective GEF proteins.

PubMed: 17292842
DOI: 10.1016/j.str.2007.01.003

実験手法

X-RAY DIFFRACTION (3 Å)