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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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Citations
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Metal nanostructures as antibacterial agents

TL;DR: In this chapter, several phenomena associated with cell damage will be explored and the influence of osmotic stress to the surface structure of bacterial cells cause pits and wrinkled protrusions, leading to increased permeability and cell death.
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Chemical Probes Reveal an Extraseptal Mode of Cross-Linking in Staphylococcus aureus

TL;DR: The results challenge the long-held belief that peptidoglycan synthesis is restricted to the septum in spherical bacteria, and instead indicate the presence of two spatiotemporally distinct modes of cross-linking in S. aureus: one at the sePTum during cell division, and another at the peripheral wall between divisions.
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A novel in vivo cell-wall labeling approach sheds new light on peptidoglycan synthesis in Escherichia coli.

TL;DR: It is shown that Escherichia coli is able to import exogenous added murein tripeptide labeled with N‐7‐nitro‐2,1,3‐benzoxadiazol‐4‐yl (AeK–NBD) into the cytoplasm where it enters the peptidoglycan biosynthesis route, resulting in fluorescent labels specifically located in the cell wall.
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PBP 4 Mediates High-Level Resistance to New-Generation Cephalosporins in Staphylococcus aureus

TL;DR: It is shown that S. aureus can also express high-level resistance to β-lactams, including new-generation broad-spectrum cephalosporins that are active against methicillin-resistant strains through an uncanonical core genome-encoded penicillin binding protein, PBP 4, a nonessential enzyme previously considered not to be important for staphylococcal β- lactam resistance.
References
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Book

Handbook of proteolytic enzymes

TL;DR: In this paper, Serine Peptidases with a Ser/Lys Catalytic Dyad (SC) are described, as well as their relation to the Nodavirus Coat Protein.

The Handbook of proteolytic enzymes

TL;DR: (Abbreviated Contents Including Section Headings:)
Journal ArticleDOI

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.
Journal ArticleDOI

Growth of the Stress-Bearing and Shape-Maintaining Murein Sacculus of Escherichia coli

TL;DR: A model is presented that postulates that maintenance of bacterial shape is achieved by the enzyme complex copying the preexisting murein sacculus that plays the role of a template.
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