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
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References
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TL;DR: This work describes the previously uncharacterized PASTA domain and infer that it binds β-lactam antibiotics and their peptidoglycan analogues, and postulates that PknB-like kinases are key regulators of cell-wall biosynthesis.
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TL;DR: The structure of PBP2x reveals an active site similar to those of the class A beta-lactamases, albeit with an absence of unambiguous deacylation machinery.
Journal ArticleDOI
Penicillin-Binding Proteins of Gram-Negative Bacteria
Brian G. Spratt,Karen D. Cromie +1 more
TL;DR: Evidence is provided that these groups of enzymes have a common, but distant, evolutionary origin, and that penicillin-resistant PBPs have arisen from the introduction of multiple amino acid substitutions within the transpeptidase domain of the enzymes.
Journal ArticleDOI
The Escherichia coli Cell Division Protein FtsW Is Required To Recruit Its Cognate Transpeptidase, FtsI (PBP3), to the Division Site
Keri Nace Mercer,David S. Weiss +1 more
TL;DR: It is suggested that a primary function of FtsW homologues--which are found in almost all bacteria and appear to work in conjunction with dedicated transpeptidases involved in division, elongation, or sporulation--is to recruit their cognate transpepticases to the correct subcellular location.
Journal ArticleDOI
Temperature-Sensitive Cell Division Mutants of Escherichia coli with Thermolabile Penicillin-Binding Proteins
TL;DR: Examination of temperature-sensitive cell division mutants of Escherichia coli provides extremely strong evidence that the inactivation of PBP3 at 42 degrees C in the mutants is the cause of the inhibition of cell division at this temperature and identifies P BP3 as an essential component of the process of celldivision in E. coli.