5BO8: Structure Of Human Sialyltransferase St8siaiii

Citation:
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-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.
PDB ID: 5BO8Download
MMDB ID: 131017
PDB Deposition Date: 2015/5/27
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 5BO8: dimeric; determined by author and by software (PISA)
Molecular Components in 5BO8
Label Count Molecule
Proteins (2 molecules)
2
Sia-alpha-2,3-gal-beta-1,4-glcnac-r:alpha 2,8- Sialyltransferase(Gene symbol: ST8SIA3)
Molecule annotation
Chemicals (20 molecules)
1
15
2
2
3
1
4
1
5
1
* Click molecule labels to explore molecular sequence information.

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