7z99: Difference between revisions

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-'''Unreleased structure'''
-The entry 7z99 is ON HOLD  until Paper Publication
+==Crystal structure of F191M variant of Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with methyl phenyl sulfoxide==
+<StructureSection load='7z99' size='340' side='right'caption='[[7z99]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7z99]] 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=7Z99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z99 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>, <scene name='pdbligand=IH0:[(S)-methylsulfinyl]benzene'>IH0</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=7z99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z99 OCA], [https://pdbe.org/7z99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z99 RCSB], [https://www.ebi.ac.uk/pdbsum/7z99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z99 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7z99" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Variovorax paradoxus EPS]]
+[[Category: Kratky J]]
+[[Category: Strater N]]
+[[Category: Weisse R]]