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.read more
Citations
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Deleting mrdA and mrcB to significantly improve extracellular recombinant protein production in Escherichia coli
TL;DR: Two key genes involved in cell wall biosynthesis were deleted (singly and doubly) in Escherichia coli, and the effects on extracellular recombinant protein production were investigated.
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Crystal Structures of Penicillin-Binding Protein D2 from Listeria monocytogenes and Structural Basis for Antibiotic Specificity.
TL;DR: The study provides the structural basis for the inhibition of PBPD2 by clinically important β-lactam antibiotics that are commonly used in listeriosis treatment and implies that the modification of β-Lactam side chains based on structural complementarity could be useful for the development of potent inhibitors against β- lactam-resistant PBPs.
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Mutations in PBP2 from ceftriaxone-resistant Neisseria gonorrhoeae alter the dynamics of the β3–β4 loop to favor a low-affinity drug-binding state
Benjamin A. Fenton,Joshua Tomberg,Carly A. Sciandra,Robert A. Nicholas,Christopher Davies,Pei Zhou +5 more
TL;DR: In this paper, the authors used solution NMR, X-ray crystallography, and isothermal titration calorimetry to find that penicillin-binding protein 2 (PBP2) can exchange dynamically between a low-affinity state with an extended β3-β4 loop conformation and a high-affiency state with a inward β3−β4 conformation.
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The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains
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References
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Peptidoglycan types of bacterial cell walls and their taxonomic implications.
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.
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.