View source for 7vqk


==Catalytic manifolds of a FMN-dependent oxidoreductase RubE7, expanding the functional diversity of the flavoenzyme superfamily==
<StructureSection load='7vqk' size='340' side='right'caption='[[7vqk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vqk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._KIB-H033 Streptomyces sp. KIB-H033]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VQK 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7vqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vqk OCA], [https://pdbe.org/7vqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vqk RCSB], [https://www.ebi.ac.uk/pdbsum/7vqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vqk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3N6GWZ7_9ACTN A0A3N6GWZ7_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flavin-dependent enzymes enable a broad range of redox transformations and generally act as monofunctional and stereoselective catalysts. Herein, we report the investigation of a multifunctional and non-stereoselective FMN-dependent oxidoreductase RubE7 from the rubrolone biosynthetic pathway. Our study outlines a single RubE7-catalysed sequential reduction of three spatially distinct bonds in a tropolone ring and a reversible double-bond reduction and dehydrogenation. The crystal structure of IstO (a RubE7 homologue) with 2.0 A resolution reveals the location of the active site at the interface of two monomers, and the size of active site is large enough to permit both flipping and free rotation of the substrate, resulting in multiple nonselective reduction reactions. Molecular docking and site mutation studies demonstrate that His106 is oriented towards the substrate and is important for the reverse dehydrogenation reaction.

Characterization of Multifunctional and Non-stereoselective Oxidoreductase RubE7/IstO, Expanding the Functional Diversity of the Flavoenzyme Superfamily.,Yan Y, Yu Z, Zhong W, Hou X, Tao Q, Cao M, Wang L, Cai X, Rao Y, Huang SX Angew Chem Int Ed Engl. 2022 May 2;61(19):e202200189. doi: , 10.1002/anie.202200189. Epub 2022 Feb 28. PMID:35191152<ref>PMID:35191152</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vqk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. KIB-H033]]
[[Category: Huang SX]]
[[Category: Yan YJ]]