› 2ilv

X-ray diffraction
2.27Å resolution

crystal structure of multifunctional sialyltransferase from Pasteurella multocida with CMP and alpha-lactose bound

Released:
DOI: 10.2210/pdb2ilv/pdb
PDB entry 2ilv coloured by chain, front view.
PDB entry 2ilv coloured by chain, side view.
PDB entry 2ilv coloured by chain, top view.
Source organism: Pasteurella multocida
Primary publication:
Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanism.
Ni L, Chokhawala HA, Cao H, Henning R, Ng L, Huang S, Yu H, Chen X, Fisher AJ
Biochemistry 46 6288-98 (2007)
PMID: 17487984

Function and Biology Details

Reaction catalysed: 
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-2,3/2,6-sialyltransferase/sialidase Chain: A
Molecule details ›
Chain: A
Length: 400 amino acids
Theoretical weight: 46.6 KDa
Source organism: Pasteurella multocida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15KI8 (Residues: 26-412; Coverage: 94%)
Sequence domains: Sialyltransferase PMO188
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, GAL
Carbohydrate polymer
1 bound ligand:
Ligand C5P 1 x C5P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 61.912Å b: 63.627Å c: 63.782Å
α: 90° β: 98.36° γ: 90°
R-values:
R R work R free
0.219 0.217 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
14 more

3 mentions without citation

Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems.
Hombu et al. (2021)
2 more