Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 22, Issue 8, Pages 627-635Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3060
Keywords
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Funding
- Consortium for Functional Glycomics [GM62116, GM098791]
- Canadian Institutes of Health Research
- Howard Hughes Medical Institute International Senior Scholar program
- Canadian Foundation of Innovation and British Columbia Knowledge Development Fund
- Tier 1 Canada Research Chairs
- Michael Smith Foundation for Health Research
- Canadian Department for Foreign Affairs and International Trade
- Deutsche Forschungsgemeinschaft
- Cystic Fibrosis Canada Fellowship
- Ministry of Science and Technology, Taiwan [NSC-103-2917-I-564-009]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM062116, R24GM098791] Funding Source: NIH RePORTER
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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-angstrom 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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