2F9G

Crystal structure of Fus3 phosphorylated on Tyr182

2F9G の概要

• エントリーDOI: 10.2210/pdb2f9g/pdb
• 関連するPDBエントリー: 2B9F 2F49 2FA2
• 分子名称: Mitogen-activated protein kinase FUS3, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: map kinase, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P16892
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41358.50

構造登録者

Bhattacharyya, R.P.,Remenyi, A.,Good, M.C.,Bashor, C.J.,Falick, A.M.,Lim, W.A. (登録日: 2005-12-05, 公開日: 2006-11-14, 最終更新日: 2024-10-30)

主引用文献

Bhattacharyya, R.P.,Remenyi, A.,Good, M.C.,Bashor, C.J.,Falick, A.M.,Lim, W.A.
The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway.
Science, 311:822-826, 2006

PubMed Abstract: Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.

PubMed: 16424299
DOI: 10.1126/science.1120941

実験手法

X-RAY DIFFRACTION (2.1 Å)