Crystallization and preliminary crystallographic analysis of the transpeptidase domain of penicillin-binding protein 2B from Streptococcus pneumoniae

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 64; no. 4; pp. 284 - 288
• Main Authors: Yamada, Mototsugu, Watanabe, Takashi, Baba, Nobuyoshi, Miyara, Takako, Saito, Jun, Takeuchi, Yasuo
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.04.2008
• Subjects: ANTIBIOTICS; Bacterial Proteins - biosynthesis; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; cell wall; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CROSS-LINKING; CRYSTALLIZATION; Crystallization Communications; Crystallography, X-Ray; CRYSTALS; DIFFRACTION; MOLECULES; Penicillin-Binding Proteins - biosynthesis; Penicillin-Binding Proteins - chemistry; Penicillin-Binding Proteins - genetics; peptidoglycan synthesis; Peptidyl Transferases - biosynthesis; Peptidyl Transferases - chemistry; Peptidyl Transferases - genetics; PRECURSOR; PROTEINS; RESOLUTION; SOLVENTS; SPACE GROUPS; Streptococcus pneumoniae - chemistry; Streptococcus pneumoniae - enzymology; β-lactams
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309108006374

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 P43212, 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.