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5bo8

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Revision as of 06:01, 7 June 2023

Structure of human sialyltransferase ST8SiaIII

Structural highlights

5bo8 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5bo8"

Categories: Homo sapiens | Large Structures | Strynadka NCJ | Volkers G | Worrall L

@@ Line 3: / Line 3: @@
 <StructureSection load='5bo8' size='340' side='right'caption='[[5bo8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5bo8]] 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=5BO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BO8 FirstGlance]. <br>
+<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>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bo6|5bo6]], [[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=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>
-<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=5bo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bo8 OCA], [http://pdbe.org/5bo8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bo8 RCSB], [http://www.ebi.ac.uk/pdbsum/5bo8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bo8 ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 20: @@
 ==See Also==
-*[[Sialyltransferase|Sialyltransferase]]
+*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Strynadka, N C.J]]
+[[Category: Strynadka NCJ]]
-[[Category: Volkers, G]]
+[[Category: Volkers G]]
-[[Category: Worrall, L]]
+[[Category: Worrall L]]
-[[Category: Sialyltransferase]]
-[[Category: Transferase]]

5bo8

From Proteopedia

Revision as of 06:01, 7 June 2023

Structure of human sialyltransferase ST8SiaIII

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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