Crystallization and initial X-ray diffraction study of the three PASTA domains of the Ser/Thr kinase Stk1 from the human pathogen Staphylococcus aureus.
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.
Paracuellos
Patricia
P
Institut de Biologie et Chimie des Protéines, UMR CNRS Université de Lyon, France.
Ballandras
Allison
A
Robert
Xavier
X
Cozzone
Alain J
AJ
Duclos
Bertrand
B
Gouet
Patrice
P
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000235:genetics; D013211:Staphylococcus aureus / Q000201:enzymology*; D037521:Virulence Factors / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D037521:Virulence Factors; D017346:Protein Serine-Threonine Kinases; C546823:Stk1 protein, Staphylococcus aureus