Crystallization and preliminary crystallographic analysis of the transpeptidase domain of penicillin-binding protein 2B from Streptococcus pneumoniae.
Penicillin-binding protein (PBP) 2B from Streptococcus pneumoniae catalyzes the cross-linking of peptidoglycan precursors that occurs during bacterial cell-wall biosynthesis. A selenomethionyl (SeMet) substituted PBP 2B transpeptidase domain was isolated from a limited proteolysis digest of a soluble form of recombinant PBP 2B and then crystallized. The crystals belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 86.39, c = 143.27 A. Diffraction data were collected to 2.4 A resolution using the BL32B2 beamline at SPring-8. The asymmetric unit contains one protein molecule and 63.7% solvent.
Yamada
Mototsugu
M
Pharmaceutical Research Center, Meiji Seika Kaisha Ltd, 760 Morooka-cho, Kohoku-ku, Yokohama 222-8567, Japan. mototsugu_yamada@meiji.co.jp
Watanabe
Takashi
T
Baba
Nobuyoshi
N
Miyara
Takako
T
Saito
Jun
J
Takeuchi
Yasuo
Y
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D046915:Penicillin-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D010458:Peptidyl Transferases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D013296:Streptococcus pneumoniae / Q000737:chemistry* / Q000201:enzymology*
D001426:Bacterial Proteins; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases