View source for 8gqr


==Crystal structure of VioD with FAD==
<StructureSection load='8gqr' size='340' side='right'caption='[[8gqr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8gqr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Duganella_sp._ZLP-XI Duganella sp. ZLP-XI]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GQR 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]] 2.1&#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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8gqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gqr OCA], [https://pdbe.org/8gqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gqr RCSB], [https://www.ebi.ac.uk/pdbsum/8gqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gqr ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Violacein is a pigment synthesized by gram-negative bacteria with various biological activities such as antimicrobial, antiviral, and anticancer activities. VioD is a key oxygenase converting protodeoxyviolaceinic acid to protoviolaceinic acid in violacein biosynthesis. To elucidate the catalytic mechanism of VioD, here, we resolved two crystal structures of VioD, a binary complex structure containing VioD and a FAD and a ternary complex structure composed of VioD, a FAD and a 2-ethyl-1-hexanol (EHN). Structural analysis revealed a deep funnel like binding pocket with wide entrance, this pocket is positively charged. The EHN is located at the deep bottom of the binding pocket near isoalloxazine ring. Further docking simulation help us to propose the mechanism of the hydroxylation of the substrate catalyzed by VioD. Bioinformatic analysis suggested and emphasized the importance of the conserved residues involved in substrate binding. Our results provide a structural basis for the catalytic mechanism of VioD.

Structural basis for substrate binding and catalytic mechanism of the key enzyme VioD in the violacein synthesis pathway.,Xu M, Xu D, Gao M, Zhuang X, Wang W, Sun B, Ran T Proteins. 2023 Mar 4. doi: 10.1002/prot.26484. PMID:36869636<ref>PMID:36869636</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8gqr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Duganella sp. ZLP-XI]]
[[Category: Large Structures]]
[[Category: Ran T]]
[[Category: Wang W]]
[[Category: Xu M]]