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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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Dissertation

Host-Pathogen Interactions in Pseudomonas aeruginosa Invasive and Respiratory Tract Infection

TL;DR: Interactions between the host and bacteria are multifaceted and P. aeruginosa utilizes outer membrane proteins and vesicles to protect against the attacks of the human immune system.
Journal ArticleDOI

Allosteric activation of cell wall synthesis during bacterial growth

TL;DR: In this paper , the peptidoglycan (PG) cell wall protects bacteria against osmotic lysis and determines cell shape, making this structure a key antibiotic target, but the molecular mechanism by which these reactions are initiated and coupled is unclear.
Dissertation

Population structure and species description of aquatic Sphingomonadaceae

Hong Chen
TL;DR: The data suggest that the incipient sexual isolation of subpopulations of freshwater Sphingomonadaceae is caused by natural selection rather than genetic drift or demographic effects, and represents a novel standard in microbial molecular systematics.
Journal ArticleDOI

MSMEG_2432 of Mycobacterium smegmatis mc2155 is a dual function enzyme that exhibits DD-carboxypeptidase and β-lactamase activities.

TL;DR: The inferred function of a putative LMM-PBP, MSMEG_2432 of Mycobacterium smegmatis, is a dual function enzyme that possesses both dd-CPase and β-lactamase activities, which is found apparent that D169A substitution in MSMEG-2432 influences both of its in vivo and in vitrodd-CPasing activities.
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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