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| | <StructureSection load='7d3a' size='340' side='right'caption='[[7d3a]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='7d3a' size='340' side='right'caption='[[7d3a]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7d3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_plauti"_(sic)_seguin_1928 "bacillus plauti" (sic) seguin 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D3A FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D3A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGI:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE'>AGI</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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]] 2.552Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGI:5,7-DIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE'>AGI</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A4U99_05915, ERS852544_00852, GXM20_05520 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292800 "Bacillus plauti" (sic) Seguin 1928])</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=7d3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d3a OCA], [https://pdbe.org/7d3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d3a RCSB], [https://www.ebi.ac.uk/pdbsum/7d3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d3a ProSAT]</span></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=7d3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d3a OCA], [https://pdbe.org/7d3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d3a RCSB], [https://www.ebi.ac.uk/pdbsum/7d3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d3a ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hong, S]] | + | [[Category: Hong S]] |
| - | [[Category: Yang, G H]] | + | [[Category: Yang GH]] |
| - | [[Category: Zhang, P]] | + | [[Category: Zhang P]] |
| - | [[Category: Apigenin]]
| + | |
| - | [[Category: Flavone reductase]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Fmn]]
| + | |
| Structural highlights
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang G, Hong S, Yang P, Sun Y, Wang Y, Zhang P, Jiang W, Gu Y. Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria. Nat Commun. 2021 Feb 4;12(1):790. doi: 10.1038/s41467-021-20974-2. PMID:33542233 doi:http://dx.doi.org/10.1038/s41467-021-20974-2
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