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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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Journal ArticleDOI

Self-resistance in Streptomyces, with Special Reference to β-Lactam Antibiotics

Hiroshi Ogawara
- 10 May 2016 - 
TL;DR: This paper emphasizes that the resistance mechanisms in Streptomyces are very hard to deal with, despite great efforts in finding new antibiotics.
Journal ArticleDOI

MtrA Response Regulator Controls Cell Division and Cell Wall Metabolism and Affects Susceptibility of Mycobacteria to the First Line Antituberculosis Drugs

TL;DR: A gain-of-function mutant, MtrAY 102C, is used, which functions in the absence of the cognate MtrB sensor kinase, to show that the MtrA regulon includes several genes involved in the processes of cell division and cell wall metabolism.
Journal ArticleDOI

Conserved mechanism of cell-wall synthase regulation revealed by the identification of a new PBP activator in Pseudomonas aeruginosa.

TL;DR: It is shown that Pseudomonas aeruginosa and other Gram-negative bacteria use the distinct lipoprotein called LpoP to activate their PBPs via a mechanism similar to LpoB-PBP activation in E. coli, indicating that it may be possible to develop broad-spectrum inhibitors of Gram- negative PBP activation despite their use of diverse PBP regulators.
Journal ArticleDOI

A Fly on the Wall: How Stress Response Systems Can Sense and Respond to Damage to Peptidoglycan

TL;DR: The current knowledge of cell wall defects sensing by stress response systems, mainly in the model bacterium Escherichia coli are explored, including how these systems can respond to cell wall perturbations to increase fitness, and what implications this has on cell wall regulation.
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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