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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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Transferable vancomycin resistance in clade B commensal-type Enterococcus faecium

TL;DR: A case of vancomycin resistance in a commensal lineage of E. faecium responsible for an atypical bacteraemia in an immunocompromised patient is reported, and a reservoir of transferable glycopeptide resistance in the community could pose a concern for public health.
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Targeting the Bacterial Transglycosylase: Antibiotic Development from a Structural Perspective.

TL;DR: The structural studies of this protein are reviewed and recent progress in developing its specific inhibitors are summarized, including synthetic substrate analogs and novel compounds identified from high-throughput screens.
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Identification of MltG as a Prc Protease Substrate Whose Dysregulation Contributes to the Conditional Growth Defect of Prc-Deficient Escherichia coli.

TL;DR: MltG is a lytic transglycosylase involved in the biogenesis of peptidoglycan (PG), suggesting a potential role of Prc in regulating PG biogenesis, and previously identified physiological Prc substrates MepS and PBP3 are involved in PGBiogenesis.
Journal ArticleDOI

Novel single-nucleotide variations associated with vancomycin resistance in vancomycin-intermediate Staphylococcus aureus.

TL;DR: Analysis of nucleotide sequence variations in 30 vancomycin-sensitive S. aureus (VSSA) and heterogeneous VISA (hVISA) and 16 VISA isolates revealed 29 single-nucleotide variations in 12 genes that are related to cell wall synthesis or the two-component system.
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PBP1a-Deficiency Causes Major Defects in Cell Division, Growth and Biofilm Formation by Streptococcus mutans

TL;DR: The results presented here highlight the importance of pbp1a in cell morphology, stress tolerance, and biofilm formation in S. mutans.
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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