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==Structure of human sialyltransferase ST8SiaIII== | ==Structure of human sialyltransferase ST8SiaIII== | ||
<StructureSection load='5bo8' size='340' side='right' caption='[[5bo8]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='5bo8' size='340' side='right'caption='[[5bo8]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bo8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BO8 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5bo8]] 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=5BO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BO8 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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.7Å</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bo8 OCA], [https://pdbe.org/5bo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bo8 RCSB], [https://www.ebi.ac.uk/pdbsum/5bo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bo8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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;"> | |||
== 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<ref>PMID:26192331</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5bo8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Strynadka NCJ]] | ||
[[Category: | [[Category: Volkers G]] | ||
[[Category: | [[Category: Worrall L]] | ||
Latest revision as of 11:28, 27 September 2023
Structure of human sialyltransferase ST8SiaIIIStructure of human sialyltransferase ST8SiaIII
Structural highlights
FunctionSIA8C_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 PubMedSialyltransferases 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 AlsoReferences
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