ArticleProceedings of the National Academy of Sciences of the United States of America2006
Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed, 361 citations in OpenAlex.
- Pro-197 mutations confer resistance to thiencarbazone but not to foramsulfuron in ALS-resistant Poa annua populations.Pest management science · 2026Article
- Synthesis, Herbicidal Activity Evaluation, and Molecular Docking of Novel Acylthioureas as AHAS Inhibitors.Molecules (Basel, Switzerland) · 2026Article
- Isoform-specific function underlies differential herbicide resistance of the W574L mutation in peanut AhALS isozymes.Pest management science · 2026Article
- Cloning and functional verification of endogenous U6 promoters for developing an efficient CRISPR/Cas9-mediated genome editing system in kenaf (Hibiscus cannabinus L.).BMC plant biology · 2026Article
- Design and evolution of the tetracycline repressor into sulfonylurea herbicide-responsive gene switches for field crops.Nature communications · 2026Article
- Genetic Origin ofPlants (Basel, Switzerland) · 2026Article
- Banana aroma is a result of acetohydroxyacid synthase and isopropylmalate synthase alternative isoforms that bypass feedback inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Synthesis and Herbicidal Activity of NovelMolecules (Basel, Switzerland) · 2026Article
- Cloning and functional verification of endogenous U6 promoters for developing an efficient CRISPR/Cas9-mediated genome editing system in kenaf (Hibiscus cannabinus L.).Research square · 2026Article
- AHAS structural changes caused by mutations result in differences in binding affinity and resistance to two herbicides inFrontiers in plant science · 2026Article
- Generating Broad-Spectrum Resistance to ALS-Inhibiting Herbicides in Rice by CRISPR/Cas9-Mediated NHEJ.Rice (New York, N.Y.) · 2025Article
- Molecular Mechanisms of Herbicide Resistance in Rapeseed: Current Status and Future Prospects for Resistant Germplasm Development.International journal of molecular sciences · 2025Review
- Development and Breeding of Herbicide-Resistant Sorghum for Effective Cereal-Legume Intercropping.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Fruits Produce Branched-Chain Esters Primarily from Newly Synthesized Precursors.Journal of agricultural and food chemistry · 2025Article
- Discovery of a New Class of Lipophilic Pyrimidine-Biphenyl Herbicides Using an Integrated Experimental-Computational Approach.Molecules (Basel, Switzerland) · 2024Article
- Distribution and Mechanism of Japanese Brome (Plants (Basel, Switzerland) · 2024Article
- The Pro-197-Thr mutation in theFrontiers in plant science · 2024Article
- Article
- Trp-574-Leu and the novel Pro-197-His/Leu mutations contribute to penoxsulam resistance inFrontiers in plant science · 2024Article
- A Double Mutation in thePlants (Basel, Switzerland) · 2023Article
27 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
The sulfonylureas and imidazolinones are potent commercial herbicide families. They are among the most popular choices for farmers worldwide, because they are nontoxic to animals and highly selective. These herbicides inhibit branched-chain amino acid biosynthesis in plants by targeting acetohydroxyacid synthase (AHAS, EC 2.2.1.6). This report describes the 3D structure of Arabidopsis thaliana AHAS in complex with five sulfonylureas (to 2.5 A resolution) and with the imidazolinone, imazaquin (IQ; 2.8 A). Neither class of molecule has a structure that mimics the substrates for the enzyme, but both inhibit by blocking a channel through which access to the active site is gained. The sulfonylureas approach within 5 A of the catalytic center, which is the C2 atom of the cofactor thiamin diphosphate, whereas IQ is at least 7 A from this atom. Ten of the amino acid residues that bind the sulfonylureas also bind IQ. Six additional residues interact only with the sulfonylureas, whereas there are two residues that bind IQ but not the sulfonylureas. Thus, the two classes of inhibitor occupy partially overlapping sites but adopt different modes of binding. The increasing emergence of resistant weeds due to the appearance of mutations that interfere with the inhibition of AHAS is now a worldwide problem. The structures described here provide a rational molecular basis for understanding these mutations, thus allowing more sophisticated AHAS inhibitors to be developed. There is no previously described structure for any plant protein in complex with a commercial herbicide.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.