› 2wlc

X-ray diffraction
1.95Å resolution

Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY

Released:
DOI: 10.2210/pdb2wlc/pdb
PDB entry 2wlc coloured by chain, front view.
PDB entry 2wlc coloured by chain, side view.
PDB entry 2wlc 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 Chain: A
Molecule details ›
Chain: A
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 ACT 3 x ACT
Ligand EDO 5 x EDO
Ligand PO4 5 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: F4132
Unit cell:
a: 199.635Å b: 199.635Å c: 199.635Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.209
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Regulation of capsule in Neisseria meningitidis.
Tzeng et al. (2016)
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