View source for 6qgm


==VirX1 apo structure==
<StructureSection load='6qgm' size='340' side='right'caption='[[6qgm]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qgm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanophage_Syn10 Cyanophage Syn10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QGM 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]] 2.75&#8491;</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=6qgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qgm OCA], [https://pdbe.org/6qgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qgm RCSB], [https://www.ebi.ac.uk/pdbsum/6qgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qgm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M4SKV1_9CAUD M4SKV1_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oceanic cyanobacteria are the most abundant oxygen-generating phototrophs on our planet and are therefore important to life. These organisms are infected by viruses called cyanophages, which have recently shown to encode metabolic genes that modulate host photosynthesis, phosphorus cycling and nucleotide metabolism. Herein we report the characterization of a wild-type flavin-dependent viral halogenase (VirX1) from a cyanophage. Notably, halogenases have been previously associated with secondary metabolism, tailoring natural products. Exploration of this viral halogenase reveals it capable of regioselective halogenation of a diverse range of substrates with a preference for forming aryl iodide species; this has potential implications for the metabolism of the infected host. Until recently, a flavin-dependent halogenase that is capable of iodination in vitro had not been reported. VirX1 is interesting from a biocatalytic perspective as it shows strikingly broad substrate flexibility and a clear preference for iodination, as illustrated by kinetic analysis. These factors together render it an attractive tool for synthesis.

A marine viral halogenase that iodinates diverse substrates.,Gkotsi DS, Ludewig H, Sharma SV, Connolly JA, Dhaliwal J, Wang Y, Unsworth WP, Taylor RJK, McLachlan MMW, Shanahan S, Naismith JH, Goss RJM Nat Chem. 2019 Oct 14. pii: 10.1038/s41557-019-0349-z. doi:, 10.1038/s41557-019-0349-z. PMID:31611633<ref>PMID:31611633</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qgm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cyanophage Syn10]]
[[Category: Large Structures]]
[[Category: Gkotsi DS]]
[[Category: Goss RJM]]
[[Category: Ludewig H]]
[[Category: McLachlan MMW]]
[[Category: Naismith JH]]
[[Category: Shanahan S]]
[[Category: Sharma SV]]
[[Category: Taylor RJK]]
[[Category: Unsworth WP]]