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| | <StructureSection load='5ax7' size='340' side='right'caption='[[5ax7]], [[Resolution|resolution]] 2.46Å' scene=''> | | <StructureSection load='5ax7' size='340' side='right'caption='[[5ax7]], [[Resolution|resolution]] 2.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ax7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. 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> | + | <table><tr><td colspan='2'>[[5ax7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pvg1, SPAC8F11.10c, SPACUNK4.18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=5ax7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ax7 OCA], [https://pdbe.org/5ax7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ax7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ax7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ax7 ProSAT]</span></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ax7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fission yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Higuchi, Y]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Kakuta, Y]] | + | [[Category: Higuchi Y]] |
| - | [[Category: Kanekiyo, M]] | + | [[Category: Kakuta Y]] |
| - | [[Category: Takegawa, K]] | + | [[Category: Kanekiyo M]] |
| - | [[Category: Yoritsune, K]] | + | [[Category: Takegawa K]] |
| - | [[Category: Yoshinaga, S]] | + | [[Category: Yoritsune K]] |
| - | [[Category: Pyruvylation]]
| + | [[Category: Yoshinaga S]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PVG1_SCHPO Involved in cell wall biogenesis. Has a role in the addition of Gal-beta1,3 moieties to galactomannans and their subsequent pyruvylation.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Andreishcheva EN, Kunkel JP, Gemmill TR, Trimble RB. Five genes involved in biosynthesis of the pyruvylated Galbeta1,3-epitope in Schizosaccharomyces pombe N-linked glycans. J Biol Chem. 2004 Aug 20;279(34):35644-55. Epub 2004 Jun 1. PMID:15173185 doi:http://dx.doi.org/10.1074/jbc.M403574200
- ↑ Higuchi Y, Yoshinaga S, Yoritsune K, Tateno H, Hirabayashi J, Nakakita S, Kanekiyo M, Kakuta Y, Takegawa K. A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide. Sci Rep. 2016 May 19;6:26349. doi: 10.1038/srep26349. PMID:27194449 doi:http://dx.doi.org/10.1038/srep26349
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