Purification, crystallization and preliminary X-ray crystallographic analysis of PBP4 from Listeria monocytogenes.

Jae Hee Jeong, Ji Eun Bae, Yeon Gil Kim

Index: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67(Pt 10) , 1247-9, (2011)

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Abstract

Penicillin-binding proteins (PBPs), which catalyze peptidoglycan synthesis, have been extensively studied as a well established target of antimicrobial agents, including β-lactam derivatives. However, remarkable resistance to β-lactams has developed among pathogenic bacteria since the clinical use of penicillin began. Recently, the glycosyltransferase (GT) domain of class A PBPs has been proposed as an attractive target for antibiotic development as moenomycin-bound GT-domain structures have been determined. In this study, a class A PBP4 from Listeria monocytogenes was overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. Diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The crystal belonged to the primitive orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 84.6, b = 127.8, c = 54.9 Å. The structural information will contribute to the further development of moenomycin-derived antibiotics possessing broad-spectrum activity.© 2011 International Union of Crystallography. All rights reserved.