4xlo
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4xlo is ON HOLD Authors: Teufel, R. Description: Crystal Structure of EncM (crystallized with 4 mM NADPH) Category: Unreleased Structures [[Cat...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==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 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='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='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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9KHK2_9ACTN Q9KHK2_9ACTN] | ||
| + | <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> | |
| - | [[Category: | + | </div> |
| - | [[Category: Teufel | + | <div class="pdbe-citations 4xlo" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces maritimus]] | ||
| + | [[Category: Teufel R]] | ||
Current revision
Crystal Structure of EncM (crystallized with 4 mM NADPH)
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