5m9x
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol== | |
| + | <StructureSection load='5m9x' size='340' side='right' caption='[[5m9x]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m9x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M9X FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7KP:(2~{R},3~{S},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-[3-[(~{E})-2-(4-hydroxyphenyl)ethenyl]-5-oxidanyl-phenoxy]oxane-3,4,5-triol'>7KP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c8b|5c8b]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.7 2.4.1.7] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9x OCA], [http://pdbe.org/5m9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m9x RCSB], [http://www.ebi.ac.uk/pdbsum/5m9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Here we present a point mutation-triggered domain shift which switches the acceptor preference of a sucrose phosphorylase from phosphate to a variety of large polyphenolic compounds including resveratrol and quercetin, enabling their efficient glucosylation. The variant possesses a high affinity for aromatic substrates due to newly introduced pi-pi- and hydrophobic interactions in the altered active site. The domain shift brings about a substantially enlarged and multifunctional active site for polyphenol glucosylation and rare disaccharide production. The crystal structure of the variant with its product resveratrol-3-alpha-d-glucoside allows the prediction of the substrate scope and regioselectivity of the aromatic compounds' glucosylation sites. | ||
| - | + | Switching enzyme specificity from phosphate to resveratrol glucosylation.,Kraus M, Grimm C, Seibel J Chem Commun (Camb). 2017 Nov 9;53(90):12181-12184. doi: 10.1039/c7cc05993k. PMID:29057405<ref>PMID:29057405</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5m9x" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Transferase]] | ||
[[Category: Grimm, C]] | [[Category: Grimm, C]] | ||
| + | [[Category: Kraus, M]] | ||
| + | [[Category: Enzyme design]] | ||
| + | [[Category: Resveratrol]] | ||
| + | [[Category: Sucrose phosphorylase]] | ||
Revision as of 06:05, 20 December 2017
Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol
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