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| | ==Structure of human sialyltransferase ST8SiaIII in complex with CDP== | | ==Structure of human sialyltransferase ST8SiaIII in complex with CDP== |
| - | <StructureSection load='5bo6' size='340' side='right' caption='[[5bo6]], [[Resolution|resolution]] 2.07Å' scene=''> | + | <StructureSection load='5bo6' size='340' side='right'caption='[[5bo6]], [[Resolution|resolution]] 2.07Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bo6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BO6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5bo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BO6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bo8|5bo8]], [[5bo7|5bo7]], [[5bo9|5bo9]]</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=5bo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bo6 OCA], [https://pdbe.org/5bo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bo6 RCSB], [https://www.ebi.ac.uk/pdbsum/5bo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bo6 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST8SIA3, SIAT8C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5bo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bo6 OCA], [http://pdbe.org/5bo6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bo6 RCSB], [http://www.ebi.ac.uk/pdbsum/5bo6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bo6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIA8C_HUMAN SIA8C_HUMAN]] May transfer sialic acid through alpha-2,8-linkages to alpha-2,3-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.<ref>PMID:10766765</ref> <ref>PMID:9826427</ref> | + | [https://www.uniprot.org/uniprot/SIA8C_HUMAN SIA8C_HUMAN] May transfer sialic acid through alpha-2,8-linkages to alpha-2,3-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.<ref>PMID:10766765</ref> <ref>PMID:9826427</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5bo6" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5bo6" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Strynadka, N C.J]] | + | [[Category: Large Structures]] |
| - | [[Category: Volkers, G]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Worrall, L]] | + | [[Category: Volkers G]] |
| - | [[Category: Cdp]] | + | [[Category: Worrall L]] |
| - | [[Category: Sialyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SIA8C_HUMAN May transfer sialic acid through alpha-2,8-linkages to alpha-2,3-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.[1] [2]
Publication Abstract from PubMed
Sialyltransferases of the mammalian ST8Sia family catalyze oligo- and polysialylation of surface-localized glycoproteins and glycolipids through transfer of sialic acids from CMP-sialic acid to the nonreducing ends of sialic acid acceptors. The crystal structure of human ST8SiaIII at 1.85-A resolution presented here is, to our knowledge, the first solved structure of a polysialyltransferase from any species, and it reveals a cluster of polysialyltransferase-specific structural motifs that collectively provide an extended electropositive surface groove for binding of oligo-polysialic acid chain products. The ternary complex of ST8SiaIII with a donor sugar analog and a sulfated glycan acceptor identified with a sialyltransferase glycan array provides insight into the residues involved in substrate binding, specificity and sialyl transfer.
Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation.,Volkers G, Worrall LJ, Kwan DH, Yu CC, Baumann L, Lameignere E, Wasney GA, Scott NE, Wakarchuk W, Foster LJ, Withers SG, Strynadka NC Nat Struct Mol Biol. 2015 Jul 20. doi: 10.1038/nsmb.3060. PMID:26192331[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Angata K, Suzuki M, McAuliffe J, Ding Y, Hindsgaul O, Fukuda M. Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III. J Biol Chem. 2000 Jun 16;275(24):18594-601. PMID:10766765 doi:http://dx.doi.org/10.1074/jbc.M910204199
- ↑ Lee YC, Kim YJ, Lee KY, Kim KS, Kim BU, Kim HN, Kim CH, Do SI. Cloning and expression of cDNA for a human Sia alpha 2,3Gal beta 1, 4GlcNA:alpha 2,8-sialyltransferase (hST8Sia III). Arch Biochem Biophys. 1998 Dec 1;360(1):41-6. PMID:9826427 doi:http://dx.doi.org/10.1006/abbi.1998.0909
- ↑ Volkers G, Worrall LJ, Kwan DH, Yu CC, Baumann L, Lameignere E, Wasney GA, Scott NE, Wakarchuk W, Foster LJ, Withers SG, Strynadka NC. Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation. Nat Struct Mol Biol. 2015 Jul 20. doi: 10.1038/nsmb.3060. PMID:26192331 doi:http://dx.doi.org/10.1038/nsmb.3060
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