5ax7
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==yeast pyruvyltransferase Pvg1p== | |
| + | <StructureSection load='5ax7' size='340' side='right' caption='[[5ax7]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ax7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AX7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ax7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ax7 OCA], [http://pdbe.org/5ax7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ax7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ax7 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PVG1_SCHPO PVG1_SCHPO]] Involved in cell wall biogenesis. Has a role in the addition of Gal-beta1,3 moieties to galactomannans and their subsequent pyruvylation.<ref>PMID:15173185</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pyruvylation onto the terminus of oligosaccharide, widely seen from prokaryote to eukaryote, confers negative charges on the cell surface and seems to be functionally similar to sialylation, which is found at the end of human-type complex oligosaccharide. However, detailed molecular mechanisms underlying pyruvylation have not been clarified well. Here, we first determined the crystal structure of fission yeast pyruvyltransferase Pvg1p at a resolution of 2.46 A. Subsequently, by combining molecular modeling with mutational analysis of active site residues, we obtained a Pvg1p mutant (Pvg1p(H168C)) that efficiently transferred pyruvyl moiety onto a human-type complex glycopeptide. The resultant pyruvylated human-type complex glycopeptide recognized similar lectins on lectin arrays as the alpha2,6-sialyl glycopeptides. This newly-generated pyruvylation of human-type complex oligosaccharides would provide a novel method for glyco-bioengineering. | ||
| - | + | A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide.,Higuchi Y, Yoshinaga S, Yoritsune K, Tateno H, Hirabayashi J, Nakakita S, Kanekiyo M, Kakuta Y, Takegawa K Sci Rep. 2016 May 19;6:26349. doi: 10.1038/srep26349. PMID:27194449<ref>PMID:27194449</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ax7" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Higuchi, Y]] | [[Category: Higuchi, Y]] | ||
[[Category: Kakuta, Y]] | [[Category: Kakuta, Y]] | ||
| + | [[Category: Kanekiyo, M]] | ||
[[Category: Takegawa, K]] | [[Category: Takegawa, K]] | ||
[[Category: Yoritsune, K]] | [[Category: Yoritsune, K]] | ||
| + | [[Category: Yoshinaga, S]] | ||
| + | [[Category: Pyruvylation]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 15:19, 20 June 2016
yeast pyruvyltransferase Pvg1p
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