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
Citations
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Molecular Basis and Phenotype of Methicillin Resistance in Staphylococcus aureus and Insights into New β-Lactams That Meet the Challenge
TL;DR: The structure and synthesis of the S. aureus cell wall, the resistance to β-lactam antibiotics through the acquisition of PBP 2a, the evolution of MRSA, and the involvement of other protein factors in methicillin resistance are discussed.
Journal ArticleDOI
Regulation of bacterial cell wall growth
TL;DR: Only now are the authors beginning to appreciate how these multiple levels of regulating PG synthesis enable the cell to propagate robustly with a defined cell shape under different and variable growth conditions.
Journal ArticleDOI
Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis.
Pradeep Kumar,Kriti Arora,John R. Lloyd,Ill Young Lee,Vinod Nair,Elizabeth R. Fischer,Helena I. Boshoff,Clifton E. Barry +7 more
TL;DR: The results suggest that the rapid lysis of meropenem‐treated cells is the result of synergistically inhibiting the transpeptidases that introduce 3,3‐cross‐links while simultaneously limiting the pool of available substrates available for cross‐linking.
Journal ArticleDOI
Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.
TL;DR: Depending on the selective β-lactam, different combinations of PBP genes and mutations within are involved in conferring resistance, and astoundingly in non-PBP genes as well.
Journal ArticleDOI
Profiling of β-Lactam Selectivity for Penicillin-Binding Proteins in Escherichia coli Strain DC2
Ozden Kocaoglu,Erin E. Carlson +1 more
TL;DR: This study evaluated 22 commercially available β-lactams for inhibition of the PBPs in live Escherichia coli strain DC2 and observed diverse PBP selectivities, with amdinocillin (mecillinam) showing selectivity for PBP2.
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.