View source for 6kqw


==Crystal structure of Yijc from B. subtilis==
<StructureSection load='6kqw' size='340' side='right'caption='[[6kqw]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KQW 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]] 2.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=6kqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqw OCA], [https://pdbe.org/6kqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kqw RCSB], [https://www.ebi.ac.uk/pdbsum/6kqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NDPGT_BACSU NDPGT_BACSU] Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids, phenyl ketones, curcuminoid, lignins, zingerone, triterpenes, stilbene and anthraquinone, using UDP-glucose or ADP-glucose as sugar donor (PubMed:28315700, PubMed:33152360). It also exhibits O-, N- and S-glycosylation activities towards simple aromatics (PubMed:28315700). In vivo, the broad acceptor tolerance of YjiC might function as a detoxification agent against exogenous xenobiotics to make the strain adaptable to the changeable environment (Probable).<ref>PMID:28315700</ref> <ref>PMID:33152360</ref> <ref>PMID:28315700</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycosylation catalyzed by uridine diphosphate-dependent glycosyltransferases (UGT) contributes to the chemical and functional diversity of a number of natural products. Bacillus subtilis Bs-YjiC is a robust and versatile UGT that holds potentials in the biosynthesis of unnatural bioactive ginsenosides. To understand the molecular mechanism underlying the substrate promiscuity of Bs-YjiC, we solved crystal structures of Bs-YjiC and its binary complex with uridine diphosphate (UDP) at resolution of 2.18 A and 2.44 A, respectively. Bs-YjiC adopts the classical GT-B fold containing the N-terminal and C-terminal domains that accommodate the sugar acceptor and UDP-glucose, respectively. Molecular docking indicates that the spacious sugar-acceptor binding pocket of Bs-YjiC might be responsible for its broad substrate spectrum and unique glycosylation patterns toward protopanaxadiol-(PPD) and PPD-type ginsenosides. Our study reveals the structural basis for the aglycone promiscuity of Bs-YjiC and will facilitate the protein engineering of Bs-YjiC to synthesize novel bioactive glycosylated compounds.

Structural dissection of unnatural ginsenoside-biosynthetic UDP-glycosyltransferase Bs-YjiC from Bacillus subtilis for substrate promiscuity.,Dai L, Qin L, Hu Y, Huang JW, Hu Z, Min J, Sun Y, Guo RT Biochem Biophys Res Commun. 2021 Jan 1;534:73-78. doi:, 10.1016/j.bbrc.2020.11.104. Epub 2020 Dec 10. PMID:33310191<ref>PMID:33310191</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kqw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Chen CC]]
[[Category: Dai LH]]
[[Category: Guo RT]]
[[Category: Hu YM]]
[[Category: Huang JW]]
[[Category: Liu WD]]