6lf6: Difference between revisions
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<StructureSection load='6lf6' size='340' side='right'caption='[[6lf6]], [[Resolution|resolution]] 2.04Å' scene=''> | <StructureSection load='6lf6' size='340' side='right'caption='[[6lf6]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6lf6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6lf6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LF6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.044Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lf6 OCA], [https://pdbe.org/6lf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lf6 RCSB], [https://www.ebi.ac.uk/pdbsum/6lf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lf6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/708A6_MAIZE 708A6_MAIZE] Bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids. Converts 2-hydroxynaringenin to isovitexin. Converts eriodictyol to orientin and isoorientin. Converts naringenin and eriodictyol to naringenin 7-O-glucoside and eriodictyol 7-O-glucoside, respectively.<ref>PMID:24045947</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6lf6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6lf6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Zea mays]] | ||
[[Category: Gao | [[Category: Gao HM]] | ||
[[Category: Yun | [[Category: Yun CH]] | ||
Latest revision as of 13:59, 22 November 2023
Crystal structure of ZmCGTa in complex with UDPCrystal structure of ZmCGTa in complex with UDP
Structural highlights
Function708A6_MAIZE Bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids. Converts 2-hydroxynaringenin to isovitexin. Converts eriodictyol to orientin and isoorientin. Converts naringenin and eriodictyol to naringenin 7-O-glucoside and eriodictyol 7-O-glucoside, respectively.[1] Publication Abstract from PubMedSchaftoside and isoschaftoside are bioactive natural products widely distributed in higher plants including cereal crops and medicinal herbs. Their biosynthesis may be related with plant defense. However, little is known on the glycosylation biosynthetic pathway of these flavonoid di-C-glycosides with different sugar residues. Herein, we report that the biosynthesis of (iso)schaftosides is sequentially catalyzed by two C-glycosyltransferases (CGTs), i.e., CGTa for C-glucosylation of the 2-hydroxyflavanone aglycone and CGTb for C-arabinosylation of the mono-C-glucoside. The two enzymes of the same plant exhibit high homology but remarkably different sugar acceptor and donor selectivities. A total of 14 CGTa and CGTb enzymes were cloned and characterized from seven dicot and monocot plants, including Scutellaria baicalensis, Glycyrrhiza uralensis, Oryza sativa ssp. japonica, and Zea mays, and the in vivo functions for three enzymes were verified by RNA interference and overexpression. Through transcriptome analysis, we found homologous genes in 119 other plants, indicating this pathway is general for the biosynthesis of (iso)schaftosides. Furthermore, we resolved the crystal structures of five CGTs and realized the functional switch of SbCGTb to SbCGTa by structural analysis and mutagenesis of key amino acids. The CGT enzymes discovered in this paper allow efficient synthesis of (iso)schaftosides, and the general glycosylation pathway presents a platform to study the chemical defense mechanisms of higher plants. Dissection of the general two-step di-C-glycosylation pathway for the biosynthesis of (iso)schaftosides in higher plants.,Wang ZL, Gao HM, Wang S, Zhang M, Chen K, Zhang YQ, Wang HD, Han BY, Xu LL, Song TQ, Yun CH, Qiao X, Ye M Proc Natl Acad Sci U S A. 2020 Nov 16. pii: 2012745117. doi:, 10.1073/pnas.2012745117. PMID:33199630[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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