The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

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ID: 295749
2008
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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.
Reference Key
openalex_W2105999876 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors E. Sauvage, Frédéric Kerff, Mohammed Terrak, Juan A. Ayala, P. Charlier
Journal FEMS microbiology reviews
Year 2008
DOI
10.1111/j.1574-6976.2008.00105.x
URL
https://academic.oup.com/femsre/article-pdf/32/2/234/8431604/32-2-234.pdf
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