Open AccessCrystallization and preliminary crystallographic analysis of the transpeptidase domain of penicillin‐binding protein 2B from Streptococcus pneumoniae
Author(s) -
Yamada Mototsugu,
Watanabe Takashi,
Baba Nobuyoshi,
Miyara Takako,
Saito Jun,
Takeuchi Yasuo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108006374
Subject(s) - penicillin binding proteins , streptococcus pneumoniae , crystallization , peptidoglycan , recombinant dna , penicillin , cell wall , proteolysis , chemistry , microbiology and biotechnology , biochemistry , crystallography , biology , antibiotics , enzyme , organic chemistry , gene
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 P 4 3 2 1 2, with unit‐cell parameters a = b = 86.39, c = 143.27 Å. Diffraction data were collected to 2.4 Å resolution using the BL32B2 beamline at SPring‐8. The asymmetric unit contains one protein molecule and 63.7% solvent.