7stq
From Proteopedia
(Difference between revisions)
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==Crystal structure of arabidopsis thaliana acetohydroxyacid synthase W574L mutant in complex with chlorimuron-ethyl== | ==Crystal structure of arabidopsis thaliana acetohydroxyacid synthase W574L mutant in complex with chlorimuron-ethyl== | ||
| - | <StructureSection load='7stq' size='340' side='right'caption='[[7stq]]' scene=''> | + | <StructureSection load='7stq' size='340' side='right'caption='[[7stq]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7STQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7STQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7stq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7STQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7STQ FirstGlance]. <br> |
| - | </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=7stq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7stq OCA], [https://pdbe.org/7stq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7stq RCSB], [https://www.ebi.ac.uk/pdbsum/7stq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7stq ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIE:2-[[[[(4-CHLORO-6-METHOXY-2-PYRIMIDINYL)AMINO]CARBONYL]AMINO]SULFONYL]BENZOIC+ACID+ETHYL+ESTER'>CIE</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TZD:2-{3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-4-METHYL-2-OXO-2,3-DIHYDRO-1,3-THIAZOL-5-YL}ETHYL+TRIHYDROGEN+DIPHOSPHATE'>TZD</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=7stq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7stq OCA], [https://pdbe.org/7stq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7stq RCSB], [https://www.ebi.ac.uk/pdbsum/7stq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7stq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ILVB_ARATH ILVB_ARATH] Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis.<ref>PMID:16665813</ref> <ref>PMID:2336405</ref> [:]<ref>PMID:16667374</ref> <ref>PMID:16668488</ref> <ref>PMID:8913312</ref> <ref>PMID:9355748</ref> <ref>PMID:9677339</ref> <ref>PMID:10386618</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acetohydroxyacid synthase (AHAS) is the target for more than 50 commercial herbicides; first applied to crops in the 1980s. Since then, 197 site-of-action resistance isolates have been identified in weeds, with mutations at P197 and W574 the most prevalent. Consequently, AHAS is at risk of not being a useful target for crop protection. To develop new herbicides, a functional understanding to explain the effect these mutations have on activity is required. Here, we show that these mutations can have two effects (i) to reduce binding affinity of the herbicides and (ii) to abolish time-dependent accumulative inhibition, critical to the exceptional effectiveness of this class of herbicide. In the two mutants, conformational changes occur resulting in a loss of accumulative inhibition by most herbicides. However, bispyribac, a bulky herbicide is able to counteract the detrimental effects of these mutations, explaining why no site-of-action resistance has yet been reported for this herbicide. | ||
| + | |||
| + | Structural basis of resistance to herbicides that target acetohydroxyacid synthase.,Lonhienne T, Cheng Y, Garcia MD, Hu SH, Low YS, Schenk G, Williams CM, Guddat LW Nat Commun. 2022 Jun 11;13(1):3368. doi: 10.1038/s41467-022-31023-x. PMID:35690625<ref>PMID:35690625</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7stq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng Y]] | [[Category: Cheng Y]] | ||
[[Category: Guddat LW]] | [[Category: Guddat LW]] | ||
Current revision
Crystal structure of arabidopsis thaliana acetohydroxyacid synthase W574L mutant in complex with chlorimuron-ethyl
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