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Open AccessJournal ArticleDOI

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

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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Journal ArticleDOI

The Bacterial Cell Envelope

TL;DR: The bacteria cell envelope is a complex multilayered structure that serves to protect these organisms from their unpredictable and often hostile environment.
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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

The oyster genome reveals stress adaptation and complexity of shell formation

TL;DR: The sequencing and assembly of the oyster genome using short reads and a fosmid-pooling strategy and transcriptomes of development and stress response and the proteome of the shell are reported, showing that shell formation in molluscs is more complex than currently understood and involves extensive participation of cells and their exosomes.
Journal ArticleDOI

Three Decades of β-Lactamase Inhibitors

TL;DR: In this paper, the authors review the catalytic mechanisms of each β-lactamase class and discuss approaches for circumventing β-latamase-mediated resistance, including properties and characteristics of mechanism-based inactivators.
Journal ArticleDOI

Bacterial peptidoglycan (murein) hydrolases.

TL;DR: The current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase is reviewed.
References
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Journal ArticleDOI

PBP1 Is a Component of the Bacillus subtilis Cell Division Machinery

TL;DR: It is shown that a PBP1 knockout strain is affected in the formation of the asymmetric sporulation septum and that green fluorescent protein-PBP1 localizes to the sporulationSeptum.
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Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase.

TL;DR: A translational pbpE-lacZ fusion was weakly expressed during vegetative growth and was significantly induced at the onset of sporulation, and depended on the activity of the spo0A product in relieving repression by the abrB repressor.
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The Crystal Structure of Phosphonate-Inhibited d-Ala-d-Ala Peptidase Reveals an Analogue of a Tetrahedral Transition State.

TL;DR: Comparisons of the structures of the DD-peptidase reaction intermediates and phosphonylated beta-lactamases show that specific substrate binding to the peptidase induces a conformational change in the active site that places Ser62 in an optimal position for catalysis.
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Penicillin-binding protein 2 genes of non-β-lactamase-producing, penicillin-resistant strains of Neisseria gonorrhoeae

TL;DR: It appears that the great majority of the altered penA genes of non‐β‐lactamase‐producing penicillin‐resistant gonococci have a clonal origin.
Journal ArticleDOI

Kinetic Characterization of the Glycosyltransferase Module of Staphylococcus aureus PBP2

TL;DR: The heterologous overexpression and purification of Staphylococcus aureus PBP2 is reported and efficient glycan polymerization from lipid II in vitro is demonstrated and enables further studies on this important class of enzymes.
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