title: Purification, crystallization and preliminary X-ray crystallographic analysis of PBP4 from Listeria monocytogenes.
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.
authors.affiliation: Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, Republic of Korea.
authors.forename: Jae Hee
authors.initials: JH
authors.lastname: Jeong
authors.forename: Ji Eun
authors.initials: JE
authors.lastname: Bae
authors.forename: Yeon Gil
authors.initials: YG
authors.lastname: Kim
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D008089:Listeria monocytogenes / Q000737:chemistry*; D046915:Penicillin-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D046915:Penicillin-Binding Proteins
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