8ET4

Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron

8ET4 の概要

• エントリーDOI: 10.2210/pdb8et4/pdb
• 関連するPDBエントリー: 5K2O
• 分子名称: Acetolactate synthase, chloroplastic, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (9 entities in total)
• 機能のキーワード: herbicide, resistance, ahas, als, ligase, transferase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66870.37

構造登録者

Guddat, L.W.,Cheng, Y. (登録日: 2022-10-16, 公開日: 2023-03-29, 最終更新日: 2024-10-16)

主引用文献

Cheng, Y.,Lonhienne, T.,Garcia, M.D.,Williams, C.M.,Schenk, G.,Guddat, L.W.
Crystal Structure of the Commercial Herbicide, Amidosulfuron, in Complex with Arabidopsis thaliana Acetohydroxyacid Synthase.
J.Agric.Food Chem., 71:5117-5126, 2023

PubMed Abstract: Amidosulfuron (AS) is from the commercial sulfonylurea herbicide family. It is highly effective against dicot broad-leaf weeds. This herbicide targets acetohydroxyacid synthase (AHAS), the first enzyme in the branched chain amino acid biosynthesis pathway. Here, we have determined the crystal structure of AS in complex with wildtype AHAS (AHAS) and with the resistance mutant, S653T. In both structures, the cofactor, ThDP, is modified to a peracetate adduct, consistent with time-dependent accumulative inhibition. Compared to other AHAS-inhibiting herbicides of the sulfonylurea family, AS lacks a second aromatic ring. The replacement is an aryl sulfonyl group with a reduced number of interactions with the enzyme and relatively low affinity ( = 4.2 μM vs low nM when two heteroaromatic rings are present). This study shows that effective herbicides can have a relatively high for plant AHAS but can still be a potent herbicide provided accumulative inhibition also occurs.

PubMed: 36943718
DOI: 10.1021/acs.jafc.2c08528

実験手法

X-RAY DIFFRACTION (2.95 Å)