Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus

Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):773-4. doi: 10.1107/S0907444904003282. Epub 2004 Mar 23.

Abstract

Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4'-phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty-acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 A, respectively. Full sets of X-ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement.

MeSH terms

  • Bacterial Proteins / chemistry
  • Cloning, Molecular
  • Crystallization*
  • Crystallography, X-Ray
  • Polyethylene Glycols
  • Sodium Chloride
  • Solvents
  • Staphylococcus aureus / enzymology*
  • Transferases (Other Substituted Phosphate Groups) / chemistry*

Substances

  • Bacterial Proteins
  • Solvents
  • Polyethylene Glycols
  • Sodium Chloride
  • Transferases (Other Substituted Phosphate Groups)
  • holo-(acyl-carrier-protein) synthase