5gl5: Difference between revisions
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==Sterol 3-beta-glucosyltransferase (ugt51) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c): UDPG complex== | ==Sterol 3-beta-glucosyltransferase (ugt51) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c): UDPG complex== | ||
<StructureSection load='5gl5' size='340' side='right' caption='[[5gl5]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5gl5' size='340' side='right'caption='[[5gl5]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5gl5]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5gl5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GL5 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]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gl5 OCA], [https://pdbe.org/5gl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gl5 RCSB], [https://www.ebi.ac.uk/pdbsum/5gl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gl5 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ATG26_YEAST ATG26_YEAST] May be involved in decane metabolism (By similarity). Involved in the biosynthesis of sterol glucoside. Not involved in autophagy-related pathways.<ref>PMID:10224056</ref> <ref>PMID:17012830</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Glycosyltransferase|Glycosyltransferase]] | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: Chen | [[Category: Chen L-Q]] | ||
[[Category: Feng | [[Category: Feng Y]] | ||
Latest revision as of 14:34, 2 August 2023
Sterol 3-beta-glucosyltransferase (ugt51) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c): UDPG complexSterol 3-beta-glucosyltransferase (ugt51) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c): UDPG complex
Structural highlights
FunctionATG26_YEAST May be involved in decane metabolism (By similarity). Involved in the biosynthesis of sterol glucoside. Not involved in autophagy-related pathways.[1] [2] Publication Abstract from PubMedSterol glycosyltransferases catalyze the formation of a variety of glycosylated sterol derivatives and are involved in producing a plethora of bioactive natural products. To understand the molecular mechanism of sterol glycosyltransferases, we determined crystal structures of a sterol glycosyltransferase UGT51 from Saccharomyces cerevisiae. The structures of the UGT51 and its complex with uridine diphosphate glucose (UDPG) were solved at resolutions of 2.77 A and 1.9 A, respectively. The structural analysis revealed that a long hydrophobic cavity, 9.2 A in width and 17.6 A in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. Furthermore, a short, conserved sequence of S847-M851 was identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations indicated that changed unique interaction network in mutant M7_1 (S(801)A/L(802)A/V(804)A/K(812)A/E(816)K/S(849)A/N(892)D), with an 1800-fold activity improvement toward an unnatural substrate protopanaxadiol (PPD), might influence its substrate preference. This study reported the first sterol glycosyltransferase structure, providing a molecular blueprint for generating tailored sterol glycosyltransferases as potential catalytic elements in synthetic biology. Structural Dissection of Sterol Glycosyltransferase UGT51 from Saccharomyces cerevisiae for Substrate Specificity.,Chen L, Zhang Y, Feng Y J Struct Biol. 2018 Nov 2. pii: S1047-8477(18)30284-3. doi:, 10.1016/j.jsb.2018.11.001. PMID:30395931[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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