7STQ

Crystal structure of arabidopsis thaliana acetohydroxyacid synthase W574L mutant in complex with chlorimuron-ethyl

Summary for 7STQ

• Entry DOI: 10.2210/pdb7stq/pdb
• Related: 5K2O
• Descriptor: Acetolactate synthase, chloroplastic, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (7 entities in total)
• Functional Keywords: herbicide, resistance, ahas, als, ligase
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 66511.25

Authors

Guddat, L.W.,Cheng, Y. (deposition date: 2021-11-15, release date: 2022-06-01, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.3 Å)