The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
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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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Journal ArticleDOI
High-Throughput Crystallography Reveals Boron-Containing Inhibitors of a Penicillin-Binding Protein with Di- and Tricovalent Binding Modes.
Hector Newman,Alen Krajnc,Dom Bellini,Charles J. Eyermann,Grant A. Boyle,Neil G. Paterson,Katherine McAuley,Robert Lesniak,Mukesh Gangar,Frank von Delft,Jürgen Brem,Kelly Chibale,Kelly Chibale,Christopher J. Schofield,Christopher G. Dowson +14 more
TL;DR: In this article, high-throughput X-ray crystallography was used to explore reactions of a boron-containing fragment set with the Pseudomonas aeruginosa PBP3 (PaPBP3).
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