6kqw: Difference between revisions
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==Crystal structure of Yijc from B. subtilis== | ==Crystal structure of Yijc from B. subtilis== | ||
<StructureSection load='6kqw' size='340' side='right'caption='[[6kqw]]' scene=''> | <StructureSection load='6kqw' size='340' side='right'caption='[[6kqw]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>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 [ | <table><tr><td colspan='2'>[[6kqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yjiC, BSU12220 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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> | </table> | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6kqw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacsu]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen | [[Category: Chen, C C]] | ||
[[Category: Dai | [[Category: Dai, L H]] | ||
[[Category: Guo | [[Category: Guo, R T]] | ||
[[Category: Hu | [[Category: Hu, Y M]] | ||
[[Category: Huang | [[Category: Huang, J W]] | ||
[[Category: Liu | [[Category: Liu, W D]] | ||
[[Category: Prenyltransferase]] | |||
[[Category: Transferase]] | |||
Revision as of 15:42, 13 October 2021
Crystal structure of Yijc from B. subtilisCrystal structure of Yijc from B. subtilis
Structural highlights
Publication Abstract from PubMedGlycosylation 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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