4xlo: Difference between revisions

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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'''


The entry 4xlo is ON HOLD
==Crystal Structure of EncM (crystallized with 4 mM NADPH)==
<StructureSection load='4xlo' size='340' side='right'caption='[[4xlo]], [[Resolution|resolution]] 1.67&Aring;' 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]] 1.67&#8491;</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.


Authors: Teufel, R.
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>


Description: Crystal Structure of EncM (crystallized with 4 mM NADPH)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Teufel, R]]
<div class="pdbe-citations 4xlo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces maritimus]]
[[Category: Teufel R]]

Latest revision as of 07:47, 27 September 2023

Crystal Structure of EncM (crystallized with 4 mM NADPH)

4xlo, resolution 1.67Å

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