6ku3
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6ku3 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of gibberellin 2-oxidase3 (GA2ox3)in rice== | |
| + | <StructureSection load='6ku3' size='340' side='right'caption='[[6ku3]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KU3 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]] 2.15Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=GA4:GIBBERELLIN+A4'>GA4</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ku3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ku3 OCA], [https://pdbe.org/6ku3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ku3 RCSB], [https://www.ebi.ac.uk/pdbsum/6ku3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ku3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Allosteric regulation is protein activation by effector binding at a site other than the active site. Here, we show via X-ray structural analysis of gibberellin 2-oxidase 3 (GA2ox3), and auxin dioxygenase (DAO), that such a mechanism maintains hormonal homeostasis in plants. Both enzymes form multimers by interacting via GA4 and indole-3-acetic acid (IAA) at their binding interface. Via further functional analyses we reveal that multimerization of these enzymes gradually proceeds with increasing GA4 and IAA concentrations; multimerized enzymes have higher specific activities than monomer forms, a system that should favour the maintenance of homeostasis for these phytohormones. Molecular dynamic analysis suggests a possible mechanism underlying increased GA2ox3 activity by multimerization-GA4 in the interface of oligomerized GA2ox3s may be able to enter the active site with a low energy barrier. In summary, homeostatic systems for maintaining GA and IAA levels, based on a common allosteric mechanism, appear to have developed independently. | ||
| - | + | A common allosteric mechanism regulates homeostatic inactivation of auxin and gibberellin.,Takehara S, Sakuraba S, Mikami B, Yoshida H, Yoshimura H, Itoh A, Endo M, Watanabe N, Nagae T, Matsuoka M, Ueguchi-Tanaka M Nat Commun. 2020 May 1;11(1):2143. doi: 10.1038/s41467-020-16068-0. PMID:32358569<ref>PMID:32358569</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ku3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Matsuoka M]] | ||
| + | [[Category: Mikami B]] | ||
| + | [[Category: Sakuraba S]] | ||
| + | [[Category: Takehara S]] | ||
| + | [[Category: Ueguchi-Tanaka M]] | ||
Current revision
Crystal structure of gibberellin 2-oxidase3 (GA2ox3)in rice
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