5man: Difference between revisions
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==Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose== | |||
<StructureSection load='5man' size='340' side='right' caption='[[5man]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5man]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MAN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NGR:3-O-ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSE'>NGR</scene></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=5man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5man OCA], [http://pdbe.org/5man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5man RCSB], [http://www.ebi.ac.uk/pdbsum/5man PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5man 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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5man" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Transferase]] | |||
[[Category: Grimm, C]] | |||
[[Category: Kraus, M]] | [[Category: Kraus, M]] | ||
[[Category: | [[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 nigerose
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