7z94: Difference between revisions
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==Crystal structure of Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with indole== | |||
<StructureSection load='7z94' size='340' side='right'caption='[[7z94]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7z94]] 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=7Z94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z94 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IND:INDOLE'>IND</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7z94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z94 OCA], [https://pdbe.org/7z94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z94 RCSB], [https://www.ebi.ac.uk/pdbsum/7z94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z94 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 7z94" 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 15:37, 22 February 2023
Crystal structure of Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with indoleCrystal structure of Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with indole
Structural highlights
FunctionPublication Abstract from PubMedFlavoprotein 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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