Crystallization and preliminary X-ray crystallographic analysis of PBPD2 from Listeria monocytogenes.
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.
Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Hyung Jin
HJ
Cha
Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Jae-Hee
JH
Jeong
Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
Yeon-Gil
YG
Kim
D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism*; D008089:Listeria monocytogenes / Q000378:metabolism*; D046915:Penicillin-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D046915:Penicillin-Binding Proteins
Listeria monocytogenes; PBPD2; penicillin-binding proteins