7es0
From Proteopedia
(Difference between revisions)
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<StructureSection load='7es0' size='340' side='right'caption='[[7es0]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='7es0' size='340' side='right'caption='[[7es0]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ES0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ES0 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3E6:Rebaudioside+A2'>3E6</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.395Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3E6:Rebaudioside+A2'>3E6</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</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=7es0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7es0 OCA], [https://pdbe.org/7es0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7es0 RCSB], [https://www.ebi.ac.uk/pdbsum/7es0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7es0 ProSAT]</span></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=7es0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7es0 OCA], [https://pdbe.org/7es0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7es0 RCSB], [https://www.ebi.ac.uk/pdbsum/7es0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7es0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Steviol glycosides are the intensely sweet components of extracts from Stevia rebaudiana. These molecules comprise an invariant steviol aglycone decorated with variable glycans and could widely serve as a low-calorie sweetener. However, the most desirable steviol glycosides Reb D and Reb M, devoid of unpleasant aftertaste, are naturally produced only in trace amounts due to low levels of specific beta (1-2) glucosylation in Stevia. Here, we report the biochemical and structural characterization of OsUGT91C1, a glycosyltransferase from Oryza sativa, which is efficient at catalyzing beta (1-2) glucosylation. The enzyme's ability to bind steviol glycoside substrate in three modes underlies its flexibility to catalyze beta (1-2) glucosylation in two distinct orientations as well as beta (1-6) glucosylation. Guided by the structural insights, we engineer this enzyme to enhance the desirable beta (1-2) glucosylation, eliminate beta (1-6) glucosylation, and obtain a promising catalyst for the industrial production of naturally rare but palatable steviol glycosides. | ||
- | + | ==See Also== | |
- | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Zhu | + | [[Category: Zhu X]] |
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Current revision
a rice glycosyltransferase in complex with UDP and REX
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