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Open AccessJournal ArticleDOI

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.

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Citations
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Journal ArticleDOI

The Bacterial Cell Envelope

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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Peptidoglycan structure and architecture

TL;DR: In several species examined, the fine structure of the peptidoglycan significantly varies with the growth conditions, and the different models for the architecture are discussed with respect to structural and physical parameters.
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The oyster genome reveals stress adaptation and complexity of shell formation

TL;DR: The sequencing and assembly of the oyster genome using short reads and a fosmid-pooling strategy and transcriptomes of development and stress response and the proteome of the shell are reported, showing that shell formation in molluscs is more complex than currently understood and involves extensive participation of cells and their exosomes.
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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.
Journal ArticleDOI

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

The biosynthesis of peptidoglycan lipid‐linked intermediates

TL;DR: This review summarizes the current knowledge on the membrane steps leading to the formation of the lipid II intermediate, i.e. the substrate of the polymerization reactions.
Journal ArticleDOI

Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism.

TL;DR: The structure and characterization of the i-Ala-(D)-meso-DAP cross-linkages between peptide subunits and the -y-carboxyl group ofglutamic acid in the link to NH2-(L-mesoDAP is revealed.
Journal ArticleDOI

Structural basis for the |[beta]| lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus

TL;DR: Structures of the acyl-PBP complexes of PBP2a with nitrocefin, penicillin G and methicillin allow, for the first time, a comparison of an apo and acylated resistant PBP.
Journal ArticleDOI

Penicillin Binding Proteins: key players in bacterial cell cycle and drug resistance processes

TL;DR: Structural, functional and biological features of penicillin-binding proteins, albeit having initially been identified several decades ago, are now being aggressively pursued as highly attractive targets for the development of novel antibiotherapies.
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