5BO9

Structure of human sialyltransferase ST8SiaIII in complex with CMP-3FNeu5Ac and Sia-6S-LacNAc

Summary for 5BO9

• Entry DOI: 10.2210/pdb5bo9/pdb
• Related: 5BO6 5BO7 5BO8
• Descriptor: Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: sialyltransferase, ternary complex, donor, acceptor, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Golgi apparatus membrane ; Single-pass type II membrane protein : O43173
• Total number of polymer chains: 2
• Total formula weight: 81544.01

Authors

Volkers, G.,Worrall, L.,Strynadka, N.C.J. (deposition date: 2015-05-27, release date: 2015-07-15, Last modification date: 2024-10-23)

Primary citation

Volkers, G.,Worrall, L.J.,Kwan, D.H.,Yu, C.C.,Baumann, L.,Lameignere, E.,Wasney, G.A.,Scott, N.E.,Wakarchuk, W.,Foster, L.J.,Withers, S.G.,Strynadka, N.C.
Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation.
Nat.Struct.Mol.Biol., 22:627-635, 2015

PubMed 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.

PubMed: 26192331
DOI: 10.1038/nsmb.3060

Experimental method

X-RAY DIFFRACTION (2.3 Å)