Crystallization and preliminary X-ray crystallographic analysis of PBPD2 from Listeria monocytogenes.

ABSTRACT: Penicillin-binding proteins (PBPs), which mediate the peptidoglycan biosynthetic pathway in the bacterial cell wall, have been intensively investigated as a target for the design of antibiotics. In this study, PBPD2, a low-molecular-weight PBP encoded by lmo2812 from Listeria monocytogenes, was overexpressed in Escherichia coli, purified and crystallized at 295?K using the sitting-drop vapour-diffusion method. The crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 37.7, b = 74.7, c = 75.1?Å, and diffracted to 1.55?Å resolution. There was one molecule in the asymmetric unit. The preliminary structure was determined by the molecular-replacement method.

SUBMITTER: Cha HJ 

PROVIDER: S-EPMC3976081 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature