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
Citations
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Toward antituberculosis drugs: in silico screening of synthetic compounds against Mycobacterium tuberculosisl,d-transpeptidase 2.
Junie B. Billones,Maria Constancia O Carrillo,Voltaire G. Organo,Macalino Stephani Joy Y,Jamie Bernadette A Sy,Inno A Emnacen,Nina Abigail B Clavio,Gisela P. Concepcion +7 more
TL;DR: In this study, structure-based pharmacophore screening, molecular docking, and in silico toxicity evaluations were employed in screening compounds from a database of synthetic compounds, and 18 structures were identified as high-scoring, high-binding hits with very satisfactory absorption, distribution, metabolism, excretion, and toxicity properties.
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Antimicrobial Activities of Zn-Doped CuO Microparticles Decorated on Polydopamine against Sensitive and Antibiotic-Resistant Bacteria
Moorthy Maruthapandi,Arumugam Saravanan,Poushali Das,Michal Natan,Gila Jacobi,Ehud Banin,John H. T. Luong,Aharon Gedanken +7 more
TL;DR: In this article, a polydopamine (PDA) composite was synthesized by depositing Zn-doped CuO (Zn@CuO) particles on PDA by one-step ultrasonication.
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Identification of MupP as a New Peptidoglycan Recycling Factor and Antibiotic Resistance Determinant in Pseudomonas aeruginosa.
TL;DR: Genetic evidence is presented that PA3172, renamed mupP, encodes the missing phosphatase predicted to function in the MurU PG recycling pathway that is widely distributed among Gram-negative bacteria.
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Kinetic Analysis of Enterococcus faecium l,d-Transpeptidase Inactivation by Carbapenems
Vincent Dubée,Michel Arthur,Michel Arthur,Michel Arthur,Hélène Fief,Sébastien Triboulet,Sébastien Triboulet,Sébastien Triboulet,Jean-Luc Mainardi,Laurent Gutmann,Matthieu Sollogoub,Louis B. Rice,Mélanie Etheve-Quelquejeu,Jean-Emmanuel Hugonnet,Jean-Emmanuel Hugonnet,Jean-Emmanuel Hugonnet +15 more
TL;DR: It is shown that the bulky side chains of commercial carbapenems have both positive and negative effects in preventing hydrolysis of the acyl enzyme and impairing drug binding in E. faecium mutants.
Journal ArticleDOI
Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein
Debanu Das,Mireille Hervé,Mireille Hervé,Julie Feuerhelm,Carol L. Farr,Hsiu-Ju Chiu,Marc-André Elsliger,Mark W. Knuth,Heath E. Klock,Mitchell D. Miller,Adam Godzik,Adam Godzik,Scott A. Lesley,Scott A. Lesley,Ashley M. Deacon,Dominique Mengin-Lecreulx,Dominique Mengin-Lecreulx,Ian A. Wilson +17 more
TL;DR: The crystal structure of the murein peptide ligase (Mpl) from the permafrost bacterium Psychrobacter arcticus 273-4 is presented and ∼30 residues that are likely to be important for recognition of the tripeptide and UDP-MurNAc substrates are identified.
References
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Peptidoglycan types of bacterial cell walls and their taxonomic implications.
Book
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Journal ArticleDOI
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