Interaction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosa.
Soluble lytic transglycosylase B1 from Pseudomonas aeruginosa was coupled to Sepharose and used to immobilize interaction partners from membrane protein extracts. Penicillin-binding protein 2 (PBP2) was identified as a binding partner, suggesting that the two proteins function together in the biosynthesis of peptidoglycan. By use of an engineered truncated derivative, the N-terminal module of PBP2 was found to confer the binding properties.
Legaree
Blaine A
BA
Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Clarke
Anthony J
AJ
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D016695:Glycosyltransferases / Q000378:metabolism*; D046915:Penicillin-Binding Proteins / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D020349:Surface Plasmon Resonance
D001426:Bacterial Proteins; D046915:Penicillin-Binding Proteins; D016695:Glycosyltransferases; C021815:murein transglycosylase