title: Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation.
abstract: 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-Å 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.
authors.affiliation: 1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Gesa
authors.initials: G
authors.lastname: Volkers
authors.affiliation: 1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Liam J
authors.initials: LJ
authors.lastname: Worrall
authors.affiliation: 1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: David H
authors.initials: DH
authors.lastname: Kwan
authors.affiliation: 1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Ching-Ching
authors.initials: CC
authors.lastname: Yu
authors.affiliation: 1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Lars
authors.initials: L
authors.lastname: Baumann
authors.affiliation: 1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Emilie
authors.initials: E
authors.lastname: Lameignere
authors.affiliation: 1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Wasney
authors.affiliation: 1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Nichollas E
authors.initials: NE
authors.lastname: Scott
authors.affiliation: Department of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
authors.forename: Warren
authors.initials: W
authors.lastname: Wakarchuk
authors.affiliation: 1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Leonard J
authors.initials: LJ
authors.lastname: Foster
authors.affiliation: 1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Stephen G
authors.initials: SG
authors.lastname: Withers
authors.affiliation: 1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
authors.forename: Natalie C J
authors.initials: NC
authors.lastname: Strynadka
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D002478:Cells, Cultured; D002855:Chromatography, Thin Layer; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D007700:Kinetics; D013058:Mass Spectrometry / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D019006:Neural Cell Adhesion Molecules / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012794:Sialic Acids / Q000737:chemistry / Q000378:metabolism*; D012799:Sialyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D019006:Neural Cell Adhesion Molecules; D011134:Polysaccharides; D011994:Recombinant Proteins; D012794:Sialic Acids; C021319:polysialic acid; C094133:Sia(alpha2,3)Gal(beta1,4)GlcNAc alpha-2,8-sialyltransferase; D012799:Sialyltransferases