6yc8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of KRED1-Pglu enzyme== | |
| + | <StructureSection load='6yc8' size='340' side='right'caption='[[6yc8]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6yc8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ogataea_glucozyma Ogataea glucozyma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YC8 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]] 1.77Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6yc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yc8 OCA], [https://pdbe.org/6yc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yc8 RCSB], [https://www.ebi.ac.uk/pdbsum/6yc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yc8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0H4SN47_9ASCO A0A0H4SN47_9ASCO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Benzil reductases are dehydrogenases preferentially active on aromatic 1,2-diketones, but the reasons for this peculiar substrate recognition have not yet been clarified. The benzil reductase (KRED1-Pglu) from the non-conventional yeast Pichia glucozyma showed excellent activity and stereoselectivity in the monoreduction of space-demanding aromatic 1,2-dicarbonyls, making this enzyme attractive as biocatalyst in organic chemistry. Structural insights into the stereoselective monoreduction of 1,2-diketones catalyzed by KRED1-Pglu were investigated starting from its 1.77 A resolution crystal structure, followed by QM and classical calculations; this study allowed for the identification and characterization of the KRED1-Pglu reactive site. Once identified the recognition elements involved in the stereoselective desymmetrization of bulky 1,2-dicarbonyls mediated by KRED1-Pglu, a mechanism was proposed together with an in silico prediction of substrates reactivity. | ||
| - | + | Structural insights into the desymmetrization of bulky 1,2-dicarbonyls through enzymatic monoreduction.,Rabuffetti M, Cannazza P, Contente ML, Pinto A, Romano D, Hoyos P, Alcantara AR, Eberini I, Laurenzi T, Gourlay L, Di Pisa F, Molinari F Bioorg Chem. 2021 Jan 11;108:104644. doi: 10.1016/j.bioorg.2021.104644. PMID:33486371<ref>PMID:33486371</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Di Pisa | + | <div class="pdbe-citations 6yc8" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ogataea glucozyma]] | ||
| + | [[Category: Di Pisa F]] | ||
Current revision
Crystal structure of KRED1-Pglu enzyme
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