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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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Journal ArticleDOI

Cloning, expression and purification of penicillin-binding protein 3 from Pseudomonas aeruginosa CMCC 10104.

TL;DR: The protocol described in this study offers a method for obtaining purified recombinant PBP3 from P. aeruginosa CMCC 10104 and indicated that the obtained rPBP3 was functional and not hindered by the presence of the C-terminal His-tag.
Dissertation

The GTP-dependant pleiotropic repressor "CodY" regulates biofilm formation in Staphylococcus aureus

Ludwig Stenz
TL;DR: In this paper, le sujet d'etude de la presente these porte sur l'analyse des fonctions du gene appele /codY /dans la formation de biofilm chez la bacterie /Staphylococcus aureus/.
Posted ContentDOI

Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli

TL;DR: This paper showed that peptidoglycan expansion requires controlled hydrolysis of cross-links and identified amongst eight endopeptidase paralogues the minimum enzyme complements essential for bacterial growth with 4[->]3 (MepM) and 3[->]-3 (mepM and mepK) crosslinks.
Journal ArticleDOI

Metabolomic profiling of polymyxin-B in combination with meropenem and sulbactam against multi-drug resistant Acinetobacter baumannii

TL;DR: Underlying mechanisms of synergistic effects of polymyxin-B combined with meropenem and sulbactam against multi-drug resistant A. baumannii are revealed, paving the way for further antibiotic penetration into bacteria cells.
Posted ContentDOI

A xylose-inducible expression system and a CRISPRi-plasmid for targeted knock-down of gene expression in Clostridioides difficile

TL;DR: New plasmid vectors that allow for titratable induction (Pxyl) or knockdown (CRISPRi) of gene expression and repression of genes in Clostridioides difficile are introduced.
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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