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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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Posted ContentDOI

The cell cycle in Staphylococcus aureus is regulated by an amidase that controls peptidoglycan synthesis

TL;DR: A membrane protein complex that spatially regulates S. aureus peptidoglycan synthesis is identified and it is shown that cell growth and division defects due to loss of this amidase can be mitigated by attenuating the polymerase activity of the major S.
Posted ContentDOI

MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling

TL;DR: In this paper, it was shown that the ReoM phosphorylation regulates peptidoglycan (PG) formation through control of MurA stability, which is the primary purpose of PrkA-mediated signaling in L. monocytogenes.
Journal ArticleDOI

Protein scaffold involving MSMEG_1285 maintains cell wall organization and mediates penicillin sensitivity in mycobacteria.

TL;DR: It is proposed that MSMEG_1285 is part of a protein scaffold, which also involves PonA1 and HbhA, and that it is responsible for the tight regulation of peptidoglycan hydrolysis.
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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