生物学
Unexpected strucuture of free plant acetohydroxyacid synthase
2017-09-23
Acetohydroxyacid synthase(AHAS,E.C.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 and imidazolinones et al.)target this enzyme.We have determined the crystal structure of a plant AHAS in the absence of any inhibitor and it shows that the herbicide-binding site adopts a foldedwhich was shown in the previous plant AHAS structures inhibited byThis is unexpected because the equivalent regions for herbicide binding in uninhibited Saccharomyces cerevisiae AHAS 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.Saccharomyces cerevisiae).The elucidation of the native structure of plant AHAS provides a new platform for future rational structure-based herbicide design efforts.
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第十届全国化学生物学学术会议报告摘要集
2017年
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