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| | <StructureSection load='4xlo' size='340' side='right'caption='[[4xlo]], [[Resolution|resolution]] 1.67Å' scene=''> | | <StructureSection load='4xlo' size='340' side='right'caption='[[4xlo]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xlo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'streptomyces_maritimus' 'streptomyces maritimus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XLO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xlo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_maritimus Streptomyces maritimus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XLO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.67Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w8w|3w8w]], [[3w8x|3w8x]], [[3w8z|3w8z]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">encM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=115828 'Streptomyces maritimus'])</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=4xlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlo OCA], [https://pdbe.org/4xlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xlo RCSB], [https://www.ebi.ac.uk/pdbsum/4xlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlo ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlo OCA], [http://pdbe.org/4xlo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xlo RCSB], [http://www.ebi.ac.uk/pdbsum/4xlo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9KHK2_9ACTN Q9KHK2_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces maritimus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Teufel, R]] | + | [[Category: Streptomyces maritimus]] |
| - | [[Category: Flavoenzyme]] | + | [[Category: Teufel R]] |
| - | [[Category: Nadph]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygenase]]
| + | |
| - | [[Category: Vanillyl-alcohol oxidase/p-cresol methylhydroxylase fold]]
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| Structural highlights
Function
Q9KHK2_9ACTN
Publication Abstract from PubMed
Flavoproteins catalyse a diversity of fundamental redox reactions and are one of the most studied enzyme families. As monooxygenases, they are universally thought to control oxygenation by means of a peroxyflavin species that transfers a single atom of molecular oxygen to an organic substrate. Here we report that the bacterial flavoenzyme EncM catalyses the peroxyflavin-independent oxygenation-dehydrogenation dual oxidation of a highly reactive poly(beta-carbonyl). The crystal structure of EncM with bound substrate mimics and isotope labelling studies reveal previously unknown flavin redox biochemistry. We show that EncM maintains an unexpected stable flavin-oxygenating species, proposed to be a flavin-N5-oxide, to promote substrate oxidation and trigger a rare Favorskii-type rearrangement that is central to the biosynthesis of the antibiotic enterocin. This work provides new insight into the fine-tuning of the flavin cofactor in offsetting the innate reactivity of a polyketide substrate to direct its efficient electrocyclization.
Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement.,Teufel R, Miyanaga A, Michaudel Q, Stull F, Louie G, Noel JP, Baran PS, Palfey B, Moore BS Nature. 2013 Nov 28;503(7477):552-6. doi: 10.1038/nature12643. Epub 2013 Oct 27. PMID:24162851[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teufel R, Miyanaga A, Michaudel Q, Stull F, Louie G, Noel JP, Baran PS, Palfey B, Moore BS. Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature. 2013 Nov 28;503(7477):552-6. doi: 10.1038/nature12643. Epub 2013 Oct 27. PMID:24162851 doi:http://dx.doi.org/10.1038/nature12643
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