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
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Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae
Tobias Dörr,Felipe Cava,Hubert Lam,Brigid M. Davis,Brigid M. Davis,Matthew K. Waldor,Matthew K. Waldor +6 more
TL;DR: Several genes in Vibrio cholerae that collectively are required for growth – particularly elongation – of this pathogen are identified and their implications for the process of side‐wall growth are discussed.
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β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.
Jed F. Fisher,Shahriar Mobashery +1 more
TL;DR: The emergence of strains of this bacterium resistant to virtually all other antibiotics has compelled the evaluation of newer β-lactam combinations as possible contributors to the multidrug chemotherapy required to control tubercular infection.
Journal ArticleDOI
Identification of a Functionally Unique Family of Penicillin-Binding Proteins
Michael Welsh,Atsushi Taguchi,Kaitlin Schaefer,Daria Van Tyne,Francois Lebreton,Michael S. Gilmore,Michael S. Gilmore,Daniel Kahne,Suzanne Walker +8 more
TL;DR: A functionally unique family of low-molecular-weight PBPs that act as transpeptidases rather than hydrolases, but they do not cross-link peptidoglycan are reported, enabling biochemical studies of proteins involved in cell wall assembly.
Journal ArticleDOI
Mecanismos de acción de los antimicrobianos
TL;DR: La sintesis proteica puede bloquearse por una amplia variedad estructural de compuestos that afectan a algunas of las fases of this proceso: activacion (mupirocina), iniciacion (oxazolidinonas, aminoglucosidos), fijacion del complejo aminoacido-ARNt al ribosoma (tetraciclinas
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HokB Monomerization and Membrane Repolarization Control Persister Awakening.
Dorien Wilmaerts,Liselot Dewachter,Pieter-Jan De Loose,Celien Bollen,Natalie Verstraeten,Jan Michiels +5 more
TL;DR: It is shown that HokB dimerization by the oxidoreductase DsbA is essential for pore formation and peptide stability, and pores are disassembled via DsbC-mediated monomerization, which targets HokB for DegQ-mediated degradation.
References
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