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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

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

Cha Hyung Jin HJ Jeong Jae-Hee JH Kim Yeon-Gil YG

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4

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 ...[more]

PMID: 24699757

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