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4xlo
From Proteopedia
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| - | ''' | + | ==Crystal Structure of EncM (crystallized with 4 mM NADPH)== |
| + | <StructureSection load='4xlo' size='340' side='right' caption='[[4xlo]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xlo]] is a 4 chain structure. 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> | ||
| + | </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> | ||
| + | <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='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://www.rcsb.org/pdb/explore.do?structureId=4xlo RCSB], [http://www.ebi.ac.uk/pdbsum/4xlo PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24162851</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Teufel, R]] | [[Category: Teufel, R]] | ||
| + | [[Category: Flavoenzyme]] | ||
| + | [[Category: Nadph]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Oxygenase]] | ||
| + | [[Category: Vanillyl-alcohol oxidase/p-cresol methylhydroxylase fold]] | ||
Revision as of 16:40, 28 January 2015
Crystal Structure of EncM (crystallized with 4 mM NADPH)
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