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

对来自人类病原体金黄色葡萄球菌的丝氨酸/苏氨酸激酶 Stk1 的三个 PASTA 结构域进行结晶和初步 X 射线衍射研究

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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.

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