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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.

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TL;DR: The bacteria cell envelope is a complex multilayered structure that serves to protect these organisms from their unpredictable and often hostile environment.
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The oyster genome reveals stress adaptation and complexity of shell formation

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Three Decades of β-Lactamase Inhibitors

TL;DR: In this paper, the authors review the catalytic mechanisms of each β-lactamase class and discuss approaches for circumventing β-latamase-mediated resistance, including properties and characteristics of mechanism-based inactivators.
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Bacterial peptidoglycan (murein) hydrolases.

TL;DR: The current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase is reviewed.
References
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Journal ArticleDOI

Structure of the low-affinity penicillin-binding protein 5 PBP5fm in wild-type and highly penicillin-resistant strains of Enterococcus faecium.

TL;DR: It appeared, with a three-dimensional model of the C-terminal domain of PBP5fm, that the substitutions of Met-485, located in the third position after the conserved SDN triad, by Thr in EFM-1 and by Ala in H80721 were the most likely cause of the decreasing affinity of P BP5fm observed in these strains.
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Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli.

TL;DR: It is concluded that Slt70, PBP7/8, and PBP3 may form a multienzyme complex in vivo.
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Mode of action of azthreonam

TL;DR: It is concluded that azthreonam, although of novel structure, has a mode of action similar to that of cephalosporins, affecting specifically septation in E. coli and most likely other gram-negative bacteria.
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Role of PBP1 in Cell Division of Staphylococcus aureus

TL;DR: Observations suggest that PBP1 is not a major contributor to the cross-linking of peptidoglycan and that its essential function must be intimately integrated into the mechanism of cell division.
Journal ArticleDOI

Common β‐lactamases inhibit bacterial biofilm formation

TL;DR: The results imply that horizontal acquisition of β‐lactamase resistance enzymes can have a phenotypic cost to bacteria by reducing their ability to form biofilms.
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