5bo8

Structure of human sialyltransferase ST8SiaIIIStructure 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.
Method:	X-ray diffraction, Resolution 2.7Å
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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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]

[2]

[3]