scispace - formally typeset
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.

read more

Citations
More filters
Book ChapterDOI

Responses of Lactic Acid Bacteria to Cell Envelope Stresses

TL;DR: An overview of the current knowledge of cell envelope stress responses in LAB is presented and the implications these responses might have with respect to antibiotic resistance development and interactions of pathogenic LAB with their hosts, the applicability of certain strains of LAB as probiotics, and the use of L AB in novel advanced applications.
Journal ArticleDOI

Crystallization and preliminary X-ray crystallographic analysis of PBPD2 from Listeria monocytogenes.

TL;DR: PBPD2, a low-molecular-weight PBP encoded by lmo2812 from Listeria monocytogenes, was overexpressed in Escherichia coli, purified and crystallized at 295 K using the sitting-drop vapour-diffusion method.
Journal ArticleDOI

Collateral Sensitivity to β-Lactam Drugs in Drug-Resistant Tuberculosis Is Driven by the Transcriptional Wiring of BlaI Operon Genes.

TL;DR: In this paper, the authors performed gene expression and network analyses and in silico knockout simulations of genes associated with β-lactam sensitivity and genes associated to resistance to classical tuberculosis drugs to investigate regulatory interactions and identify key gene mediators.
References
More filters
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.
Related Papers (5)