7U25

Crystal structure of arabidopsis thaliana acetohydroxyacid synthase W574L mutant in complex with bispyribac-sodium

7U25 の概要

• エントリーDOI: 10.2210/pdb7u25/pdb
• 関連するPDBエントリー: 5K2O
• 分子名称: Acetolactate synthase, chloroplastic, MAGNESIUM ION, 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid, ... (7 entities in total)
• 機能のキーワード: herbicide, resistance, ahas, als, ligase
• 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: 66496.46

構造登録者

Guddat, L.W.,Cheng, Y. (登録日: 2022-02-23, 公開日: 2022-06-01, 最終更新日: 2023-10-18)

主引用文献

Lonhienne, T.,Cheng, Y.,Garcia, M.D.,Hu, S.H.,Low, Y.S.,Schenk, G.,Williams, C.M.,Guddat, L.W.
Structural basis of resistance to herbicides that target acetohydroxyacid synthase.
Nat Commun, 13:3368-3368, 2022

PubMed Abstract: Acetohydroxyacid synthase (AHAS) is the target for more than 50 commercial herbicides; first applied to crops in the 1980s. Since then, 197 site-of-action resistance isolates have been identified in weeds, with mutations at P197 and W574 the most prevalent. Consequently, AHAS is at risk of not being a useful target for crop protection. To develop new herbicides, a functional understanding to explain the effect these mutations have on activity is required. Here, we show that these mutations can have two effects (i) to reduce binding affinity of the herbicides and (ii) to abolish time-dependent accumulative inhibition, critical to the exceptional effectiveness of this class of herbicide. In the two mutants, conformational changes occur resulting in a loss of accumulative inhibition by most herbicides. However, bispyribac, a bulky herbicide is able to counteract the detrimental effects of these mutations, explaining why no site-of-action resistance has yet been reported for this herbicide.

PubMed: 35690625
DOI: 10.1038/s41467-022-31023-x

実験手法

X-RAY DIFFRACTION (3.19 Å)