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Inactivation of PBP3x caused no changes in the cell morphology or growth rate of exponentially growing cells, suggesting that pbpC was not required for cell viability under normal laboratory growth conditions. By gene replacement, a PBP3x-defective interposon mutant (strain HC132) was obtained and confirmed by Southern blot analysis. aeruginosa PBP3 did, and overexpression of the pbpC gene product had no effect on the susceptibility to the PBP3-targeted antibiotics tested. penicillin-binding competition assays indicated that the pbpC gene product had lower affinities for several PBP3-targeted beta-lactam antibiotics than P. By using a broad-host-range vector, pUCP27, the pbpC gene was expressed in P. coli and was exported to the cytoplasmic membrane of E. The pbpC gene product was expressed from the T7 promoter in E. coli soxR gene and the Mycobacterium bovis adh gene. The downstream sequence of pbpC encoded convergently transcribed homologs of the E. Apo-PBP3 crystals were used for soaking the individual DBO inhibitors in mother liquor as follows. PBP3 crystals were grown via the sitting drop method using previously published conditions: 30 polyethylene glycol 4000, 0.2 M MgCl 2, 0.1 M Tris, pH 8.5.
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Analysis of the translated sequence of the pbpC gene encoding this PBP3x revealed that 41 and 48% of its amino acids were identical to those of Escherichia coli and P. aeruginosa PBP3 protein expression and purification were carried out as described earlier (24, 29, 30). A homolog of Pseudomonas aeruginosa penicillin-binding protein 3 (PBP3), named PBP3x in this study, was identified by using degenerate primers based on conserved amino acid motifs in the high-molecular-weight PBPs.