7z4x: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[7z4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Variovorax_paradoxus_EPS Variovorax paradoxus EPS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z4X FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#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=7z4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z4x OCA], [https://pdbe.org/7z4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z4x RCSB], [https://www.ebi.ac.uk/pdbsum/7z4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z4x ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/E6V140_VARPE E6V140_VARPE]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Flavoprotein monooxygenases are a versatile group of enzymes for biocatalytic transformations. Among these, group E monooxygenases (GEMs) catalyze enantioselective epoxidation and sulfoxidation reactions. Here, we describe the crystal structure of an indole monooxygenase from the bacterium Variovorax paradoxus EPS, a GEM designated as VpIndA1. Complex structures with substrates reveal productive binding modes that, in conjunction with force-field calculations and rapid mixing kinetics, reveal the structural basis of substrate and stereoselectivity. Structure-based redesign of the substrate cavity yielded variants with new substrate selectivity (for sulfoxidation of benzyl phenyl sulfide) or with greatly enhanced stereospecificity (from 35.1 % to 99.8 % ee for production of (1S,2R) indene oxide). This first determination of the substrate binding mode of GEMs combined with structure-function relationships opens the door for structure-based design of these powerful biocatalysts.
-Structural and Mechanistical Studies on Substrate and Stereo Selectivity of the Indole Monooxygenase VpIndA1: New Avenues for Biocatalytic Epoxidations and Sulfoxidations.,Kratky J, Eggerichs D, Heine T, Hofmann S, Sowa P, Weisse RH, Tischler D, Strater N Angew Chem Int Ed Engl. 2023 Feb 10:e202300657. doi: 10.1002/anie.202300657. PMID:36762980<ref>PMID:36762980</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7z4x" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>