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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

Decoding microbial genomes to understand their functional roles in human complex diseases

TL;DR: In this article , the role of the Gut Microbiome in complex diseases from a functional perspective is summarized and state-of-the-art techniques have been highlighted which may contribute to a mechanistic understanding of the gut microbiome in human complex diseases.
Journal ArticleDOI

Characterization of the proteins encoded by the Bacillus subtilis yoxA-dacC operon.

TL;DR: In Bacillus subtilis, the yoxA and dacC genes were proposed to form an operon and its product fused to a polyhistidine tag was purified and a clear dd-endopeptidase activity was obtained with this penicillin-binding protein, or PBP.
Dissertation

Characterisation of infectious bursal disease virus (IBDV) polyprotein processing.

TL;DR: It was hypothesised that VP4 exists in two forms, the embedded form which exists as an integral part of the polyprotein and a mature form which is released after the processing, which was used to identify products resulting from the IBDV polyprotein processing.
Journal ArticleDOI

Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis.

TL;DR: Structural insights lay the groundwork to develop improved beta-lactam therapeutics for tuberculosis by understanding the functional and inhibitor-binding specificities of penicillin-binding proteins from the pathogen Mycobacterium tuberculosis.
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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