› 4r83

X-ray diffraction
1.93Å resolution

Crystal structure of Sialyltransferase from Photobacterium damsela

Released:
DOI: 10.2210/pdb4r83/pdb
PDB entry 4r83 coloured by chain, front view.
PDB entry 4r83 coloured by chain, side view.
PDB entry 4r83 coloured by chain, top view.
Source organism: Photobacterium damselae
Primary publication:
Crystal structures of sialyltransferase from Photobacterium damselae.
Huynh N, Li Y, Yu H, Huang S, Lau K, Chen X, Fisher AJ
FEBS Lett 588 4720-9 (2014)
PMID: 25451227

Function and Biology Details

Reaction catalysed: 
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130302 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PhoU domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 503 amino acids
Theoretical weight: 56.83 KDa
Source organism: Photobacterium damselae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O66375 (Residues: 16-497; Coverage: 71%)
Gene name: bst
Sequence domains: Sialyltransferase PMO188
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P1
Unit cell:
a: 64.67Å b: 81.34Å c: 111.84Å
α: 98.6° β: 92.76° γ: 100.85°
R-values:
R R work R free
0.181 0.179 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Glycosyltransferases: mechanisms and applications in natural product development.
Liang et al. (2015)
1 more

2 mentions without citation

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