2F49

Crystal structure of Fus3 in complex with a Ste5 peptide

2F49 の概要

• エントリーDOI: 10.2210/pdb2f49/pdb
• 関連するPDBエントリー: 2B9F 2B9H 2B9I 2B9J
• 分子名称: Mitogen-activated protein kinase FUS3, STE5 peptide, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: protein-petide complex, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Nucleus: P16892
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 85423.05

構造登録者

Remenyi, A. (登録日: 2005-11-22, 公開日: 2006-03-28, 最終更新日: 2023-08-23)

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 (1.9 Å)