View source for 5man


==Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose==
<StructureSection load='5man' size='340' side='right'caption='[[5man]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5man]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_adolescentis Bifidobacterium adolescentis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5MAN 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]] 2.04&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900052:alpha-nigerose'>PRD_900052</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=5man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5man OCA], [https://pdbe.org/5man PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5man RCSB], [https://www.ebi.ac.uk/pdbsum/5man PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5man ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUCP_BIFAA SUCP_BIFAA] Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).<ref>PMID:14740189</ref> <ref>PMID:20691225</ref> 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5man" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bifidobacterium adolescentis]]
[[Category: Large Structures]]
[[Category: Grimm C]]
[[Category: Kraus M]]