› 2wle

X-ray diffraction
2.19Å resolution

Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY

Released:
DOI: 10.2210/pdb2wle/pdb
PDB entry 2wle coloured by chain, front view.
PDB entry 2wle coloured by chain, side view.
PDB entry 2wle coloured by chain, top view.
Source organism: Neisseria meningitidis serogroup Y
Primary publication:
Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.
Lee HJ, Rakić B, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC
J Biol Chem 284 24501-11 (2009)
PMID: 19525232

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polysialic acid O-acetyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 215 amino acids
Theoretical weight: 23.73 KDa
Source organism: Neisseria meningitidis serogroup Y
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93S40 (Residues: 1-215; Coverage: 100%)
Gene names: oatWY, siaD
Sequence domains: Bacterial transferase hexapeptide (six repeats)
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

3 bound ligands:
Ligand COA 2 x COA
Ligand EDO 2 x EDO
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: COPPER HOME SOURCE
Spacegroup: P222
Unit cell:
a: 79.074Å b: 94.523Å c: 100.886Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.242
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Biosynthesis and production of polysialic acids in bacteria.
Ferrero et al. (2010)
5 more

2 mentions without citation

Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.
Lee et al. (2009)
1 more