5yx4

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Current revision (10:25, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5yx4' size='340' side='right'caption='[[5yx4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5yx4' size='340' side='right'caption='[[5yx4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yx4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YX4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YX4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yx4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deschampsia_antarctica Deschampsia antarctica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YX4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCC:2,4,4-TRIHYDROXYCHALCONE'>HCC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yx4 OCA], [http://pdbe.org/5yx4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yx4 RCSB], [http://www.ebi.ac.uk/pdbsum/5yx4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yx4 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCC:2,4,4-TRIHYDROXYCHALCONE'>HCC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yx4 OCA], [https://pdbe.org/5yx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yx4 RCSB], [https://www.ebi.ac.uk/pdbsum/5yx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yx4 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G4U3G8_DESAN G4U3G8_DESAN]
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Chalcone isomerase (CHI) is an important enzyme for flavonoid biosynthesis that catalyzes the intramolecular cyclization of chalcones into (S)-flavanones. CHIs have been classified into two types based on their substrate specificity. Type I CHIs use naringenin chalcone as a substrate and are found in most of plants besides legumes, whereas type II CHIs in leguminous plants can also utilize isoliquiritigenin. In this study, we found that the CHI from the Antarctic plant Deschampsia antarctica (DaCHI1) is of type I based on sequence homology but can use type II CHI substrates. To clarify the enzymatic mechanism of DaCHI1 at the molecular level, the crystal structures of unliganded DaCHI1 and isoliquiritigenin-bound DaCHI1 were determined at 2.7 and 2.1 A resolutions, respectively. The structures revealed that isoliquiritigenin binds to the active site of DaCHI1 and induces conformational changes. Additionally, the activity assay showed that while DaCHI1 exhibits substrate preference for naringenin chalcone, it can also utilize isoliquiritigenin although the catalytic activity was relatively low. Based on these results, we propose that DaCHI1 uses various substrates to produce antioxidant flavonoids as an adaptation to oxidative stresses associated with harsh environmental conditions.
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Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.,Park SH, Lee CW, Cho SM, Lee H, Park H, Lee J, Lee JH PLoS One. 2018 Feb 2;13(2):e0192415. doi: 10.1371/journal.pone.0192415., eCollection 2018. PMID:29394293<ref>PMID:29394293</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yx4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
 
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[[Category: Lee, C W]]
 
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[[Category: Lee, J H]]
 
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[[Category: Park, S]]
 
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[[Category: Chalcone isomerase]]
 
[[Category: Deschampsia antarctica]]
[[Category: Deschampsia antarctica]]
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[[Category: Isomerase]]
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[[Category: Large Structures]]
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[[Category: Lee CW]]
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[[Category: Lee JH]]
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[[Category: Park S]]

Current revision

Isoliquiritigenin-complexed Chalcone isomerase (S189A) from the Antarctic vascular plant Deschampsia Antarctica (DaCHI1)

PDB ID 5yx4

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OCA

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