7d3b

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'''Unreleased structure'''
 
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The entry 7d3b is ON HOLD until Paper Publication
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==flavone reductase==
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<StructureSection load='7d3b' size='340' side='right'caption='[[7d3b]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D3B FirstGlance]. <br>
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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]] 2.25&#8491;</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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=LU2:2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-4H-CHROMEN-4-ONE'>LU2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7d3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d3b OCA], [https://pdbe.org/7d3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d3b RCSB], [https://www.ebi.ac.uk/pdbsum/7d3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d3b ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Gut microbial transformations of flavonoids, an enormous class of polyphenolic compounds abundant in plant-based diets, are closely associated with human health. However, the enzymes that initiate the gut microbial metabolism of flavones and flavonols, the two most abundant groups of flavonoids, as well as their underlying molecular mechanisms of action remain unclear. Here, we discovered a flavone reductase (FLR) from the gut bacterium, Flavonifractor plautii ATCC 49531 (originally assigned as Clostridium orbiscindens DSM 6740), which specifically catalyses the hydrogenation of the C2-C3 double bond of flavones/flavonols and initiates their metabolism as a key step. Crystal structure analysis revealed the molecular basis for the distinct catalytic property of FLR. Notably, FLR and its widespread homologues represent a class of ene-reductases that has not been previously identified. Genetic and biochemical analyses further indicated the importance of FLR in gut microbial consumption of dietary and medicinal flavonoids, providing broader insight into gut microbial xenobiotic transformations and possible guidance for personalized nutrition and medicine.
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Authors: Hong, S., Yang, G.H., Zhang, P.
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Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria.,Yang G, Hong S, Yang P, Sun Y, Wang Y, Zhang P, Jiang W, Gu Y Nat Commun. 2021 Feb 4;12(1):790. doi: 10.1038/s41467-021-20974-2. PMID:33542233<ref>PMID:33542233</ref>
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Description: flavone reductase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Yang, G.H]]
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<div class="pdbe-citations 7d3b" style="background-color:#fffaf0;"></div>
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[[Category: Zhang, P]]
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== References ==
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[[Category: Hong, S]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Hong S]]
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[[Category: Yang GH]]
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[[Category: Zhang P]]

Current revision

flavone reductase

PDB ID 7d3b

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