1JSC

Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors

1JSC の概要

• エントリーDOI: 10.2210/pdb1jsc/pdb
• 分子名称: ACETOHYDROXY-ACID SYNTHASE, POTASSIUM ION, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: acetohydroxyacid synthase, acetolactate synthase, fad, thiamin diphosphate, herbicide inhibition, lyase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion: P07342
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 139745.49

構造登録者

Pang, S.S.,Duggleby, R.G.,Guddat, L.W. (登録日: 2001-08-17, 公開日: 2002-01-16, 最終更新日: 2023-08-16)

主引用文献

Pang, S.S.,Duggleby, R.G.,Guddat, L.W.
Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.
J.Mol.Biol., 317:249-262, 2002

PubMed Abstract: Acetohydroxyacid synthase (AHAS; EC 4.1.3.18) catalyzes the first step in branched-chain amino acid biosynthesis. The enzyme requires thiamin diphosphate and FAD for activity, but the latter is unexpected, because the reaction involves no oxidation or reduction. Due to its presence in plants, AHAS is a target for sulfonylurea and imidazolinone herbicides. Here, the crystal structure to 2.6 A resolution of the catalytic subunit of yeast AHAS is reported. The active site is located at the dimer interface and is near the proposed herbicide-binding site. The conformation of FAD and its position in the active site are defined. The structure of AHAS provides a starting point for the rational design of new herbicides.

PubMed: 11902841
DOI: 10.1006/jmbi.2001.5419

実験手法

X-RAY DIFFRACTION (2.6 Å)