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
Citations
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Journal ArticleDOI
Live-Cell Profiling of Penicillin-Binding Protein Inhibitors in Escherichia coli MG1655.
TL;DR: An optimized live-cell assay for screening inhibitors of the PBPs in Escherichia coli MG1655 is developed and the utility of this assay for the screening of inhibitors in live, non-hypersusceptible Gram-negative organisms is demonstrated.
Journal ArticleDOI
Combined Structural Analysis and Molecular Dynamics Reveal Penicillin-Binding Protein Inhibition Mode with β-Lactones.
Parker Flanders,Carlos Contreras-Martel,Nathaniel W. Brown,Joshua D. Shirley,Alexandre Martins,Kelsie N Nauta,Andréa Dessen,Erin E. Carlson,Elizabeth A. Ambrose +8 more
TL;DR: A new class of β-lactone-containing molecules that interact with PBPs, often in an isoform-specific manner, and do not incorporate this C-terminal mimetic is identified, expanding the understanding of PBP inhibitor binding.
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Clinical and microbiological characterization of Aerococcus urinae bacteraemias at Helsinki metropolitan area, Finland
TL;DR: In this article , the authors evaluated the outcome of commonly used cefuroxime treatment and determinate a set of A. urinae in vitro antimicrobial susceptibilities for benzylpenicillin, cefurusime, and ceftriaxone.
Book ChapterDOI
Cell Wall Targeted Antibiotics
TL;DR: The biosynthesis of murein occurs in three stages, which take place in the cytoplasm forming muropeptide precursors, the inner side of the cy toplasmic membrane involving the undecaprenyl-phosphate carrier lipid, and the periplasm where the assembly of the macromolecule takes place.
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Mass-spectrometry analysis of genetic markers of S. pneumoniae resistance to β-lactam antibiotics
TL;DR: No association between the presence of mutations in PBP genes and decreased susceptibility to cefotaxime was shown, which makes it possible to suggest significant differences in molecular mechanisms of penicillins and cephalosporins resistance.
References
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Journal ArticleDOI
Peptidoglycan types of bacterial cell walls and their taxonomic implications.
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.
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.