5fem
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5fem is ON HOLD Authors: Guddat, L.W., Lonhienne, T. Description: Saccharomyces cerevisiae Acetohydroxyacid Synthase in complex with bensulfuron me...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Saccharomyces cerevisiae Acetohydroxyacid Synthase in complex with bensulfuron methyl== | |
| + | <StructureSection load='5fem' size='340' side='right'caption='[[5fem]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fem]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FEM FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.168Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=60G:METHYL+2-[(4,6-DIMETHOXYPYRIMIDIN-2-YL)CARBAMOYLSULFAMOYLMETHYL]BENZOATE'>60G</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fem OCA], [https://pdbe.org/5fem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fem RCSB], [https://www.ebi.ac.uk/pdbsum/5fem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fem ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ILVB_YEAST ILVB_YEAST] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26924714</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5fem" style="background-color:#fffaf0;"></div> |
| - | [[Category: Guddat | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Guddat LW]] | ||
| + | [[Category: Lonhienne T]] | ||
Current revision
Saccharomyces cerevisiae Acetohydroxyacid Synthase in complex with bensulfuron methyl
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