The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
TLDR
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.Abstract:
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.read more
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Bacterial peptidoglycan (murein) hydrolases.
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References
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Journal ArticleDOI
Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide.
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TL;DR: The crystal structure of PBP4a (encoded by the dacC gene) is solved and a binding pocket specific to the diaminopimelic acid, the third residue of the peptidoglycan stem pentapeptide of B. subtilis is revealed.
Journal ArticleDOI
Possible role of Escherichia coli penicillin-binding protein 6 in stabilization of stationary-phase peptidoglycan.
TL;DR: It is concluded that P BP6 has a biological function clearly distinct from that of PBP5 and to suggest a role for PBP6 in the stabilization of the peptidoglycan during stationary phase.
Journal ArticleDOI
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15.
TL;DR: The serinedd-transpeptidase/penicillin-binding protein of Streptomyces K15 catalyzes peptide bond formation in a way that mimics the peniillin-sensitive peptide cross-linking reaction involved in bacterial cell wall peptidoglycan assembly.
Journal ArticleDOI
The penicillin resistance of Enterococcus faecalis JH2-2r results from an overproduction of the low-affinity penicillin-binding protein PBP4 and does not involve a psr-like gene.
TL;DR: It is postulated that the PBP4 overproduction in E. faecalis JH2-2r results from the modification of an as yet unidentified factor.
Journal ArticleDOI
Structure-Activity Relationships of Different β-Lactam Antibiotics against a Soluble Form of Enterococcus faecium PBP5, a Type II Bacterial Transpeptidase
Andrea M. Hujer,Malgosia Kania,Thomas A. Gerken,Vernon E. Anderson,John D. Buynak,Xiaoxia Ge,Patrick Caspers,Malcolm G. P. Page,Louis B. Rice,Robert A. Bonomo +9 more
TL;DR: This characterization defines important structure-activity relationships for this clinically relevant type II transpeptidase, shows that the rate of formation of the acyl-enzyme is an essential factor determining the efficacy of a β-lactam, and suggests that the specific side chain interactions of β- lactams could be modified to improve inactivation of resistant PBPs.