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.read more
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Pseudomonas aeruginosa Alters Peptidoglycan Composition under Nutrient Conditions Resembling Cystic Fibrosis Lung Infections
Erin M. Anderson,Neethu Shaji Saji,Alexander C. Anderson,Dyanne Brewer,Anthony S. Clare,Cezar M. Khursigara +5 more
TL;DR: The PG composition of two P. aeruginosa epidemic strains varied significantly when grown under conditions resembling cystic fibrosis lung infections, showing increases in O-methylated stem peptides and decreases in l,d-endopeptidase activity as well as an increased abundance of de-N-acetylated sugars and l,D-transpeptid enzyme activity, which are related to bacterial virulence and antibiotic resistance, respectively.
Journal ArticleDOI
Enhanced conversion of sterols to steroid synthons by augmenting the peptidoglycan synthesis gene pbpB in Mycobacterium neoaurum
TL;DR: It is demonstrated that the modification of peptidoglycan synthesis can improve the conversion of sterols to steroid synthons in mycobacteria.
Journal ArticleDOI
The Penicillin-Binding Protein PbpP Is a Sensor of β-Lactams and Is Required for Activation of the Extracytoplasmic Function σ Factor σ P in Bacillus thuringiensis
TL;DR: This work identifies the penicillin-binding protein PbpP and demonstrates its essential role in the activation of σP, an extracytoplasmic function (ECF) σ factor that controls β-lactam resistance in the species Bacillus thuringiensis, Bacillus cereus, and Bacillus anthracis.
Journal ArticleDOI
Ptr/CTL0175 Is Required for the Efficient Recovery of Chlamydia trachomatis From Stress Induced by Gamma-Interferon.
Maria Emilia Panzetta,Maria Emilia Panzetta,Agustin Leonardo Lujan,Agustin Leonardo Lujan,Robert J. Bastidas,María T. Damiani,María T. Damiani,Raphael H. Valdivia,Hector Alex Saka,Hector Alex Saka +9 more
TL;DR: Findings indicate that the putative secreted protease Ptr is required for C. trachomatis to specifically recover from IFNγ- but not penicillin-induced stress.
Journal ArticleDOI
Synthesis of a meso-Oxa-Diaminopimelic Acid Containing Peptidoglycan Pentapeptide and Coupling to the GlcNAc-anhydro-MurNAc Disaccharide
TL;DR: The preparation of the PG pentapeptide containing the isosteric analog meso-oxa-Dap is described, which relies on the ring opening of a peptide embedded aziridine via the attack of a serine residue to produce a putative substrate for the AmpG pore protein.
References
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