Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria. This review focuses on the detailed structure of PBPs and their implication in peptidoglycan synthesis, maturation and recycling. An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria
This work was supported in part by the Europan Commission Sixth Framework Program grants LSMH-CT-COBRA 2003-503335 and LSMH-CT-EUR-INTAFAR 2004-512138, by the Belgian Program on Interuniversity Poles of Attraction initiated by the Belgian State, Prime Minister's Office, Science Policy programming (IAP no. P6/19), by the Actions de Recherche Concertées (grant 03/08-297), by the Fonds National de la Recherche Scientifique (IISN 4.4505.00, FRFC 9.45/9.99, FRFC 2.4.508.01.F, FRFC 9.4.538.03.F, FRFC 2.4.524.03) and the University of Liège (Fonds spéciaux, Crédit classique, 1999). F.K. is Chargé de Recherche and M.T. is Chercheur Qualifié of the Fonds de la Recherche Scientifique (F.R.S.-FNRS, Brussels, Belgium)
Peer reviewed