Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of PBP4 from Listeria monocytogenes
Author(s) -
Jeong JaeHee,
Bae JiEun,
Kim YeonGil
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111027400
Subject(s) - penicillin binding proteins , listeria monocytogenes , orthorhombic crystal system , penicillin , crystallization , crystallography , peptidoglycan , chemistry , antimicrobial , bacteria , cell wall , microbiology and biotechnology , antibiotics , biochemistry , biology , crystal structure , organic chemistry , genetics
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 P 2 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.