› 1kru

X-ray diffraction
2.8Å resolution

Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A

Released:
DOI: 10.2210/pdb1kru/pdb
PDB entry 1kru coloured by chain, front view.
PDB entry 1kru coloured by chain, side view.
PDB entry 1kru coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the lac operon galactoside acetyltransferase.
Wang XG, Olsen LR, Roderick SL
Structure 10 581-8 (2002)
PMID: 11937062

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139597 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactoside O-acetyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 203 amino acids
Theoretical weight: 22.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P07464 (Residues: 1-203; Coverage: 100%)
Gene names: JW0333, b0342, lacA
Sequence domains:
Structure domains: Hexapeptide repeat proteins

Ligands and Environments


Cofactor: Ligand COA 3 x COA
1 bound ligand:
Ligand IPT 6 x IPT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 66.1Å b: 183.8Å c: 121.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.172 0.247
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Modeling network dynamics: the lac operon, a case study.
Vilar et al. (2003)
2 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