6kun: Difference between revisions

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-'''Unreleased structure'''
-The entry 6kun is ON HOLD
+==Crystal structure of dioxygenase for auxin oxidation (DAO) in rice==
+<StructureSection load='6kun' size='340' side='right'caption='[[6kun]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KUN 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]] 2.002&#8491;</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IAC:1H-INDOL-3-YLACETIC+ACID'>IAC</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=6kun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kun OCA], [https://pdbe.org/6kun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kun RCSB], [https://www.ebi.ac.uk/pdbsum/6kun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kun 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6kun" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Matsuoka M]]
+[[Category: Mikami B]]
+[[Category: Sakuraba S]]
+[[Category: Takehara S]]
+[[Category: Ueguchi-Tanaka M]]