5K6Q
Crystal structure of Arabidopsis thaliana acetohydroxyacid synthase catalytic subunit
Summary for 5K6Q
| Entry DOI | 10.2210/pdb5k6q/pdb |
| Related | 1YBH 1YHY 1YHZ 1YI0 1Z8N |
| Descriptor | Acetolactate synthase, chloroplastic, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | ahas, acetohydroxyacid synthase, acetolactate synthase, herbicide, catalytic subunit, thiamin diphosphate, fad, transferase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Plastid, chloroplast : P17597 |
| Total number of polymer chains | 1 |
| Total formula weight | 66077.17 |
| Authors | Garcia, M.D.,Wang, J.-G.,Lonhienne, T.,Guddat, L.W. (deposition date: 2016-05-25, release date: 2017-05-31, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 28485824DOI: 10.1111/febs.14102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.952 Å) |
Structure validation
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