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Keywords:

  • lipid A biosynthesis;
  • LpxA;
  • UDP-N-acetylglucosamine acyltransferase;
  • antibacterial drug target;
  • Helicobactor pylori.

Lipid A, a constituent of lipopolysaccharides, is essential for the growth and virulence of most Gram-negative bacteria. This makes its biosynthetic enzymes potential targets for development of new antibacterial agents. The first step of lipid A biosynthesis is catalyzed by the enzyme UDP-N-acetylglucosamine acyltransferase (LpxA). LpxA from the pathogenic bacterium Helicobacter pylori has been overexpressed in Escherichia coli and crystallized at 297 K using ammonium sulfate and sodium/potassium tartrate as precipitants in the presence of a detergent. Diffraction data to 2.1 Å resolution have been collected from a native crystal. The crystal belongs to space group P6322, with unit-cell parameters a = b = 90.69, c = 148.20 Å. The asymmetric unit contains one subunit of LpxA, with a crystal volume per protein mass (VM) of 2.87 Å3 Da−1 and a solvent content of 57.1%.