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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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Insights into naturally minimised Streptomyces

TL;DR: S. albus J1074 carries the smallest genome among the completely sequenced species of the genus Streptomyces, and the genome revealed 22 additional putative secondary metabolite gene clusters that reinforce the strain’s potential for natural product synthesis.
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A New Covalent Inhibitor of Class C β-Lactamases Reveals Extended Active Site Specificity.

TL;DR: The new molecule proved, unexpectedly, to be a very effective inactivator of class C β-lactamases, more so than the original lead compound, O-phenoxy Carbonyl-N-(benzyloxycarbonyl)hydroxylamine, and was a mechanism-based inhibitor in which an inert complex is formed by noncovalent rearrangement.
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Distinct and Specific Role of NlpC/P60 Endopeptidases LytA and LytB in Cell Elongation and Division of Lactobacillus plantarum.

TL;DR: It is shown that LytA is required for cell elongation while LytB is involved in the spatio-temporal regulation of cell division, which confirms the key roles played by both enzymes in PG remodeling during the cell cycle of L. plantarum.
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Structural determination of archaeal UDP-N-acetylglucosamine 4-epimerase from Methanobrevibacter ruminantium M1 in complex with the bacterial cell wall intermediate UDP-N-acetylmuramic acid

TL;DR: The crystal structure of UDP-N-acetylglucosamine 4-epimerase, from the archaeal methanogen Methanobrevibacter ruminantium strain M1, was determined to a resolution of 1.65 A and contained a conserved N-terminal Rossmann-fold for nucleotide binding and an active site positioned in the C-terminus.
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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