View source for 7xre


==Crystal structure of DgpA==
<StructureSection load='7xre' size='340' side='right'caption='[[7xre]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xre]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_intestinal_bacterium_PUE Human intestinal bacterium PUE]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XRE 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]] 2.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=7xre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xre OCA], [https://pdbe.org/7xre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xre RCSB], [https://www.ebi.ac.uk/pdbsum/7xre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xre ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3Q9WWX8_UNCXX A0A3Q9WWX8_UNCXX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The C-glycosidic bond that connects the sugar moiety with aglycone is difficult to be broken or made due to its inert nature. The knowledge of C-glycoside breakdown and synthesis is very limited. Recently, the enzyme DgpA/B/C cascade from a human intestinal bacterium PUE was identified to specifically cleave the C-glycosidic bond of puerarin (daidzein-8-C-glucoside). Here we investigated how puerarin is recognized and oxidized by DgpA based on crystal structures of DgpA with or without substrate and biochemical characterization. More strikingly, we found that apart from being a C-glycoside cleaving enzyme, DgpA/B/C is capable of efficiently converting O- to C-glycoside showing the activity as a structure isomerase. A possible mechanistic model was proposed dependently of the simulated complex structure of DgpB/C with 3''-oxo-daidzin and structure-based mutagenesis. Our findings not only shed light on understanding the enzyme-mediated C-glycosidic bond breakage and formation, but also may help to facilitate stereospecific C-glycoside synthesis in pharmaceutical industry.

Structural mechanism of a dual-functional enzyme DgpA/B/C as both a C-glycoside cleaving enzyme and an O- to C-glycoside isomerase.,He P, Wang S, Li S, Liu S, Zhou S, Wang J, Tao J, Wang D, Wang R, Ma W Acta Pharm Sin B. 2023 Jan;13(1):246-255. doi: 10.1016/j.apsb.2022.05.022. Epub , 2022 May 25. PMID:36815035<ref>PMID:36815035</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xre" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human intestinal bacterium PUE]]
[[Category: Large Structures]]
[[Category: He P]]
[[Category: Ma W]]