View source for 6ing


==A complex structure of H25A mutant of glycosyltransferase with UDP==
<StructureSection load='6ing' size='340' side='right'caption='[[6ing]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ing]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stevia_rebaudiana Stevia rebaudiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ING OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ING 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]] 1.698&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=6ing FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ing OCA], [https://pdbe.org/6ing PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ing RCSB], [https://www.ebi.ac.uk/pdbsum/6ing PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ing ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U76G1_STERE U76G1_STERE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Diets high in sugar are recognized as a serious health problem, and there is a drive to reduce their consumption. Steviol glycosides are natural zero-calorie sweeteners, but the most desirable ones are biosynthesized with low yields. UGT76G1 catalyzes the beta (1-3) addition of glucose to steviol glycosides, which gives them the preferred taste. UGT76G1 is able to transfer glucose to multiple steviol substrates yet remains highly specific in the glycosidic linkage it creates. Here, we report multiple complex structures of the enzyme combined with biochemical data, which reveal that the enzyme utilizes hydrophobic interactions for substrate recognition. The lack of a strict three-dimensional recognition arrangement, typical of hydrogen bonds, permits two different orientations for beta (1-3) sugar addition. The use of hydrophobic recognition is unusual in a regio- and stereo-specific catalysis. Harnessing such non-specific hydrophobic interactions could have wide applications in the synthesis of complex glycoconjugates.

Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations.,Yang T, Zhang J, Ke D, Yang W, Tang M, Jiang J, Cheng G, Li J, Cheng W, Wei Y, Li Q, Naismith JH, Zhu X Nat Commun. 2019 Jul 19;10(1):3214. doi: 10.1038/s41467-019-11154-4. PMID:31324778<ref>PMID:31324778</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ing" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Stevia rebaudiana]]
[[Category: Naismith JH]]
[[Category: Zhu X]]