7z98
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of F191M variant Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with methyl phenyl sulfide== | |
| + | <StructureSection load='7z98' size='340' side='right'caption='[[7z98]], [[Resolution|resolution]] 1.73Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7z98]] 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=7Z98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z98 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=16R:(METHYLSULFANYL)BENZENE'>16R</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=7z98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z98 OCA], [https://pdbe.org/7z98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z98 RCSB], [https://www.ebi.ac.uk/pdbsum/7z98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z98 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7z98" 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]] | ||
Revision as of 12:37, 22 February 2023
Crystal structure of F191M variant Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with methyl phenyl sulfide
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