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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.