Crystallization and initial X-ray diffraction study of the three PASTA domains of the Ser/Thr kinase Stk1 from the human pathogen Staphylococcus aureus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1187-9. doi: 10.1107/S174430910904250X. Epub 2009 Oct 30.

Abstract

PASTA subunits (approximately 70 amino acids) are specific to bacterial serine/threonine kinases and to penicillin-binding proteins (PBPs) and are involved in the synthesis of peptidoglycan. The human pathogen Staphylococcus aureus contains a serine/threonine kinase, Stk1, which plays a major role in virulence. A recombinant His-tagged portion of the extracellular domain of Stk1 containing three PASTA subunits has been crystallized using zinc sulfate as a crystallizing agent. The crystals belonged to the tetragonal space group P4(1)22, with unit-cell parameters a = 68.0, b = 68.0, c = 158.1 angstrom. Structure determination by the MAD method is now in progress.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / genetics
  • Staphylococcus aureus / enzymology*
  • Virulence Factors / chemistry*
  • Virulence Factors / genetics
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Virulence Factors
  • Protein Serine-Threonine Kinases
  • Stk1 protein, Staphylococcus aureus