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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The Allosteric Site for the Nascent Cell Wall in Penicillin-Binding Protein 2a: An Achilles' Heel of Methicillin-Resistant Staphylococcus aureus.
TL;DR: The present knowledge of the allosteric mechanism, the conformational changes allowing PBP2a catalysis and the means by which some clinical strains have acquired resistance to ceftaroline by disrupting the allostery mechanism are summarized.
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Thermosensitive PBP2a requires extracellular folding factors PrsA and HtrA1 for Staphylococcus aureus MRSA β-lactam resistance
Melanie Roch,Emmanuelle Lelong,Olesya O. Panasenko,Roberto Sierra,Adriana Renzoni,William L. Kelley +5 more
TL;DR: It is demonstrated that extracellular protein folding factors contribute to MRSA’s resistance to β-lactam antibiotics by influencing PBP2A quality control and suggested that targeting chaperones or disrupting partially folded proteins represents an effective strategy to combat the spread of antibiotic resistance.
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Defining the regulon of genes controlled by σE, a key regulator of the cell envelope stress response in Streptomyces coelicolor
Ngat T. Tran,Xiaoluo Huang,Xiaoluo Huang,Hee-Jeon Hong,Matthew J. Bush,Govind Chandra,Daniela Pinto,Maureen J. Bibb,Matthew I. Hutchings,Thorsten Mascher,Mark J. Buttner +10 more
TL;DR: Using a combination of chromatin immunoprecipitation‐sequencing, microarray transcriptional profiling and bioinformatic analysis, biological insight is provided into the σE‐mediated cell envelope stress response in the genus Streptomyces.
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Recognition of peptidoglycan fragments by the transpeptidase PBP4 from Staphylococcus aureus
R. Maya-Martinez,J. A. N. Alexander,Christian Otten,Isabel Ayala,Daniela Vollmer,Catherine M. Bougault,A. Bert,Cédric Laguri,M. Fonvielle,Michel Arthur,Natalie C. J. Strynadka,Waldemar Vollmer,Jean-Pierre Simorre +12 more
TL;DR: Liquid-state NMR identified two interaction surfaces in close proximity to the central nucleophile position that can accommodate the potential donor and acceptor stems for the transpeptidation reaction in PBP4, which provides new mechanistic insights into mecA independent resistance to β-lactams in S. aureus.
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Lysine biosynthesis in microbes: relevance as drug target and prospects for β-lactam antibiotics production.
TL;DR: This review discusses the suitability of interrupting lysine biosynthesis as target for new antibacterial and antifungal compounds and emphasises on biochemical reactions involved in the formation of α-aminoadipate in fungi as an essential intermediate for both, l Lysine and β-lactam antibiotics production.
References
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Journal ArticleDOI
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.