2. Academic Validation
  3. Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation

Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation

  • Nat Struct Mol Biol. 2015 Aug;22(8):627-35. doi: 10.1038/nsmb.3060.
Gesa Volkers 1,  Liam J Worrall 1,  David H Kwan 2,  Ching-Ching Yu 2,  Lars Baumann 2,  Emilie Lameignere 1,  Gregory A Wasney 1,  Nichollas E Scott 2,  Warren Wakarchuk 3,  Leonard J Foster 2,  Stephen G Withers 2,  Natalie C J Strynadka 1
Affiliations

Affiliations

  • 1 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.
  • 2 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.
  • 3 Department of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
PMID: 26192331 DOI: 10.1038/nsmb.3060
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.

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