Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori
Acta Crystallographica Section D
Volume 58, Issue 5, pages 864–866, May 2002
How to Cite
Lee, B. I., Lee, J. Y., Moon, J., Han, B. W. and Suh, S. W. (2002), Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori. Acta Crystallographica Section D, 58: 864–866. doi: 10.1107/S0907444902004845
- lipid A biosynthesis;
- 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%.