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6myw
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6myw is ON HOLD Authors: Garfinkle, S.E., Jeffrey, P., Hyster, T.K. Description: Gluconobacter Ene-Reductase (GluER) mutant -T36A [[Category: Unrel...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Gluconobacter Ene-Reductase (GluER) mutant - T36A== | |
| + | <StructureSection load='6myw' size='340' side='right'caption='[[6myw]], [[Resolution|resolution]] 1.16Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6myw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gluconobacter_oxydans Gluconobacter oxydans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MYW 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]] 1.157Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6myw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6myw OCA], [https://pdbe.org/6myw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6myw RCSB], [https://www.ebi.ac.uk/pdbsum/6myw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6myw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A1E8I9_GLUOY A1E8I9_GLUOY] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Photoexcitation is a common strategy for initiating radical reactions in chemical synthesis. We found that photoexcitation of flavin-dependent "ene"-reductases changes their catalytic function, enabling these enzymes to promote an asymmetric radical cyclization. This reactivity enables the construction of five-, six-, seven-, and eight-membered lactams with stereochemical preference conferred by the enzyme active site. After formation of a prochiral radical, the enzyme guides the delivery of a hydrogen atom from flavin-a challenging feat for small-molecule chemical reagents. The initial electron transfer occurs through direct excitation of an electron donor-acceptor complex that forms between the substrate and the reduced flavin cofactor within the enzyme active site. Photoexcitation of promiscuous flavoenzymes has thus furnished a previously unknown biocatalytic reaction. | ||
| - | + | Photoexcitation of flavoenzymes enables a stereoselective radical cyclization.,Biegasiewicz KF, Cooper SJ, Gao X, Oblinsky DG, Kim JH, Garfinkle SE, Joyce LA, Sandoval BA, Scholes GD, Hyster TK Science. 2019 Jun 21;364(6446):1166-1169. doi: 10.1126/science.aaw1143. PMID:31221855<ref>PMID:31221855</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6myw" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hyster | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gluconobacter oxydans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Garfinkle SE]] | ||
| + | [[Category: Hyster TK]] | ||
| + | [[Category: Jeffrey P]] | ||
Current revision
Gluconobacter Ene-Reductase (GluER) mutant - T36A
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