5fem

Saccharomyces cerevisiae Acetohydroxyacid Synthase in complex with bensulfuron methyl

spinqualitylabelsall models 5fem, resolution 2.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fem is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.168Å Ligands: 60G, FAD, MG, TPP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ILVB_YEAST Publication Abstract from PubMed Acetohydroxyacid synthase (AHAS) inhibitors are highly successful commercial herbicides. New kinetic data show that the binding of these compounds leads to reversible accumulative inhibition of AHAS. Crystallographic data (to a resolution of 2.17 A) for an AHAS-herbicide complex shows that closure of the active site occurs when the herbicidal inhibitor binds, thus preventing exchange with solvent. This feature combined with new kinetic data shows that molecular oxygen promotes an accumulative inhibition leading to the conclusion that the exceptional potency of these herbicides is augmented by subversion of an inherent oxygenase side reaction. The reactive oxygen species produced by this reaction are trapped in the active site, triggering oxidation reactions that ultimately lead to the alteration of the redox state of the cofactor flavin adenine dinucleotide (FAD), a feature that accounts for the observed reversible accumulative inhibition. Commercial Herbicides Can Trigger the Oxidative Inactivation of Acetohydroxyacid Synthase.,Lonhienne T, Nouwens A, Williams CM, Fraser JA, Lee YT, West NP, Guddat LW Angew Chem Int Ed Engl. 2016 Mar 18;55(13):4247-51. doi: 10.1002/anie.201511985. , Epub 2016 Feb 29. PMID:26924714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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