5K6Q

Crystal structure of Arabidopsis thaliana acetohydroxyacid synthase catalytic subunit

5K6Q の概要

• エントリーDOI: 10.2210/pdb5k6q/pdb
• 関連するPDBエントリー: 1YBH 1YHY 1YHZ 1YI0 1Z8N
• 分子名称: Acetolactate synthase, chloroplastic, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: ahas, acetohydroxyacid synthase, acetolactate synthase, herbicide, catalytic subunit, thiamin diphosphate, fad, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Plastid, chloroplast : P17597
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66077.17

構造登録者

Garcia, M.D.,Wang, J.-G.,Lonhienne, T.,Guddat, L.W. (登録日: 2016-05-25, 公開日: 2017-05-31, 最終更新日: 2024-10-30)

主引用文献

Garcia, M.D.,Wang, J.G.,Lonhienne, T.,Guddat, L.W.
Crystal structure of plant acetohydroxyacid synthase, the target for several commercial herbicides.
FEBS J., 284:2037-2051, 2017

PubMed Abstract: Acetohydroxyacid synthase (AHAS, EC 2.2.1.6) is the first enzyme in the branched-chain amino acid biosynthesis pathway. Five of the most widely used commercial herbicides (i.e. sulfonylureas, imidazolinones, triazolopyrimidines, pyrimidinyl-benzoates and sulfonylamino-cabonyl-triazolinones) target this enzyme. Here we have determined the first crystal structure of a plant AHAS in the absence of any inhibitor (2.9 Å resolution) and it shows that the herbicide-binding site adopts a folded state even in the absence of an inhibitor. This is unexpected because the equivalent regions for herbicide binding in uninhibited Saccharomyces cerevisiae AHAS crystal structures are either disordered, or adopt a different fold when the herbicide is not present. In addition, the structure provides an explanation as to why some herbicides are more potent inhibitors of Arabidopsis thaliana AHAS compared to AHASs from other species (e.g. S. cerevisiae). The elucidation of the native structure of plant AHAS provides a new platform for future rational structure-based herbicide design efforts.

PubMed: 28485824
DOI: 10.1111/febs.14102

実験手法

X-RAY DIFFRACTION (2.952 Å)