6u9d
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Saccharomyces cerevisiae acetohydroxyacid synthase== |
| - | <StructureSection load='6u9d' size='340' side='right'caption='[[6u9d]]' scene=''> | + | <StructureSection load='6u9d' size='340' side='right'caption='[[6u9d]], [[Resolution|resolution]] 3.19Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6u9d]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U9D 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=6u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u9d OCA], [https://pdbe.org/6u9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u9d RCSB], [https://www.ebi.ac.uk/pdbsum/6u9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u9d 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]] 3.194Å</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=6u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u9d OCA], [https://pdbe.org/6u9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u9d RCSB], [https://www.ebi.ac.uk/pdbsum/6u9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u9d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ILVB_YEAST ILVB_YEAST] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acetohydroxyacid synthase (AHAS), also known as acetolactate synthase, is a FAD and ThDP-Mg(2+)-dependent enzyme that catalyses the first step in the biosynthesis of the branched chain amino acids (BCAAs)(1). It is the target for over 50 commercial herbicides(2). AHAS requires both catalytic and regulatory subunits for maximal activity and functionality. Herein, our structures of the hexadecameric Saccharomyces cerevisiae and dodecameric Arabidopsis thaliana AHAS complexes demonstrate that the regulatory subunits form a core upon which the catalytic subunit dimers are attached, adopting the shape of a "Maltese Cross". The structures show how the catalytic and regulatory subunits communicate with each other to provide a pathway for activation and for feedback inhibition by the BCAAs. We also show that Mycobacterium tuberculosis AHAS adopts a similar structure, thus demonstrating that the overall AHAS architecture is conserved across kingdoms. | ||
| + | |||
| + | Structures of fungal and plant acetohydroxyacid synthases.,Lonhienne T, Low YS, Garcia MD, Croll T, Gao Y, Wang Q, Brillault L, Williams CM, Fraser JA, McGeary RP, West NP, Landsberg MJ, Rao Z, Schenk G, Guddat LW Nature. 2020 Jul 8. pii: 10.1038/s41586-020-2514-3. doi:, 10.1038/s41586-020-2514-3. PMID:32640464<ref>PMID:32640464</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6u9d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| + | [[Category: Guddat LW]] | ||
| + | [[Category: Lonhienne T]] | ||
Current revision
Saccharomyces cerevisiae acetohydroxyacid synthase
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