6jen: Difference between revisions
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<StructureSection load='6jen' size='340' side='right'caption='[[6jen]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='6jen' size='340' side='right'caption='[[6jen]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jen]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JEN OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[6jen]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/American_pokeweed American pokeweed]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JEN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JEN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3RL:PTEROSTILBENE'>3RL</scene>, <scene name='pdbligand=U2F:URIDINE-5-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE'>U2F</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3RL:PTEROSTILBENE'>3RL</scene>, <scene name='pdbligand=U2F:URIDINE-5-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE'>U2F</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PaGT2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3527 American pokeweed])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jen OCA], [http://pdbe.org/6jen PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jen RCSB], [http://www.ebi.ac.uk/pdbsum/6jen PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jen ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The glycosylation of small hydrophobic compounds is catalyzed by uridine diphosphate glycosyltransferases (UGTs). Because glycosylation is an invaluable tool for improving the stability and water solubility of hydrophobic compounds, UGTs have attracted attention for their application in the food, cosmetics, and pharmaceutical industries. However, the ability of UGTs to accept and glycosylate a wide range of substrates is not clearly understood due to the existence of a large number of UGTs. PaGT2, a UGT from Phytolacca americana, can regioselectively glycosylate piceatannol but has low activity toward other stilbenoids. To elucidate the substrate specificity and catalytic mechanism, we determined the crystal structures of PaGT2 with and without substrates and performed molecular docking studies. The structures have revealed key residues involved in substrate recognition and suggest the presence of a nonconserved catalytic residue (His81) in addition to the highly conserved catalytic histidine in UGTs (His18). The role of the identified residues in substrate recognition and catalysis is elucidated with the mutational assay. Additionally, the structure-guided mutation of Cys142 to other residues, Ala, Phe, and Gln, allows PaGT2 to glycosylate resveratrol with high regioselectivity, which is negligibly glycosylated by the wild-type enzyme. These results provide a basis for tailoring an efficient glycosyltransferase. | |||
An Ambidextrous Polyphenol Glycosyltransferase PaGT2 from Phytolacca americana.,Maharjan R, Fukuda Y, Shimomura N, Nakayama T, Okimoto Y, Kawakami K, Nakayama T, Hamada H, Inoue T, Ozaki SI Biochemistry. 2020 Jul 14;59(27):2551-2561. doi: 10.1021/acs.biochem.0c00224., Epub 2020 Jul 2. PMID:32525309<ref>PMID:32525309</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6jen" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: American pokeweed]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fukuda, Y]] | [[Category: Fukuda, Y]] | ||
Revision as of 14:19, 22 July 2020
Structure of Phytolacca americana UGT2 complexed with UDP-2fluoro-glucose and pterostilbeneStructure of Phytolacca americana UGT2 complexed with UDP-2fluoro-glucose and pterostilbene
Structural highlights
Publication Abstract from PubMedThe glycosylation of small hydrophobic compounds is catalyzed by uridine diphosphate glycosyltransferases (UGTs). Because glycosylation is an invaluable tool for improving the stability and water solubility of hydrophobic compounds, UGTs have attracted attention for their application in the food, cosmetics, and pharmaceutical industries. However, the ability of UGTs to accept and glycosylate a wide range of substrates is not clearly understood due to the existence of a large number of UGTs. PaGT2, a UGT from Phytolacca americana, can regioselectively glycosylate piceatannol but has low activity toward other stilbenoids. To elucidate the substrate specificity and catalytic mechanism, we determined the crystal structures of PaGT2 with and without substrates and performed molecular docking studies. The structures have revealed key residues involved in substrate recognition and suggest the presence of a nonconserved catalytic residue (His81) in addition to the highly conserved catalytic histidine in UGTs (His18). The role of the identified residues in substrate recognition and catalysis is elucidated with the mutational assay. Additionally, the structure-guided mutation of Cys142 to other residues, Ala, Phe, and Gln, allows PaGT2 to glycosylate resveratrol with high regioselectivity, which is negligibly glycosylated by the wild-type enzyme. These results provide a basis for tailoring an efficient glycosyltransferase. An Ambidextrous Polyphenol Glycosyltransferase PaGT2 from Phytolacca americana.,Maharjan R, Fukuda Y, Shimomura N, Nakayama T, Okimoto Y, Kawakami K, Nakayama T, Hamada H, Inoue T, Ozaki SI Biochemistry. 2020 Jul 14;59(27):2551-2561. doi: 10.1021/acs.biochem.0c00224., Epub 2020 Jul 2. PMID:32525309[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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