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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycoproteins, , glycoproteins, oligo-, -
- 1. glycoproteins, , glycoproteins, polysialylation, -
- 1. polysialylation, , glycoproteins, -, -
Output(Part-Of) (sent_index,
protein,
site):
- 2. polysialyltransferase, motifs
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):