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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Cell envelope stress responses upon protein overproduction in Bacillus subtilis
TL;DR: In this paper, the onmisbaarheid van PrsA, een foldase verantwoordelijk is voor een correcte vouwing van uitgescheiden eiwitten, is onderzocht.
Journal ArticleDOI
CroR Regulates Expression of pbp4(5) to Promote Cephalosporin Resistance in Enterococcus faecalis
Sarah B Timmler,Stephanie L. Kellogg,Samantha N Atkinson,Jaime L. Little,Dušanka Djorić,Christopher J. Kristich +5 more
TL;DR: Investigation into molecular mechanisms used by enterococci to subvert cephalosporin antibiotics is imperative for preventing and treating life-threatening infections and it is found that enhanced production of the penicillin-binding protein Pbp4(5) upon exposure to cell wall stress was mediated by CroS/R and was critical for intrinsic cep Halosporins resistance of E. faecalis.
Journal ArticleDOI
Structure-based inhibitor design for reshaping bacterial morphology
Yu Mi Choi,Ji Su Park,JinShil Kim,Kyungjin Min,Kiran V. Mahasenan,Choonkeun Kim,Hyejin Yoon,Sewon Lim,Dae Hee Cheon,Yan Lee,Sangryeol Ryu,Shahriar Mobashery,B. Moon Kim,Byung Ho Lee +13 more
TL;DR: In this paper , the peptidoglycan hydrolase 3 (Pgp3) is involved in the spiral shape formation of Campylobacter jejuni, which is critical for invasion of intestinal mucosa epithelial cells.
Dissertation
Exploring the substrate specificity of the antimicrobial peptide transporter BceAB of Bacillus subtilis
TL;DR: This study investigates the substrate specificity of the transporter BceAB of Bacillus subtilis and focuses on characterising the binding capacity of its large extracellular domain in vitro and further aim to identify the physiological substrate of BCEAB using in vivo approaches.
Dissertation
Development of a method to generate a soluble substrate for lytic transglycosylases
TL;DR: A method for the generation of a soluble, homogeneous oligosaccharide substrate that can be used to study LTs is developed, based on the enzymatic degradation of peptidoglycan into fragments of aSpecies nature, and their separation by HPLC.
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.
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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.
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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.