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Chembiochem : a European Journal of... Dec 2010
Topics: Bacillus subtilis; Molecular Structure; Peptidoglycan; Spores, Bacterial
PubMed: 21117117
DOI: 10.1002/cbic.201000626 -
PloS One 2016The biosynthetic pathway of peptidoglycan, an essential component of bacterial cell wall, is a well-recognized target for antibiotic development. Peptidoglycan...
The biosynthetic pathway of peptidoglycan, an essential component of bacterial cell wall, is a well-recognized target for antibiotic development. Peptidoglycan precursors are synthesized in the bacterial cytosol by various enzymes including the ATP-hydrolyzing Mur ligases, which catalyze the stepwise addition of amino acids to a UDP-MurNAc precursor to yield UDP-MurNAc-pentapeptide. MurD catalyzes the addition of D-glutamic acid to UDP-MurNAc-L-Ala in the presence of ATP; structural and biochemical studies have suggested the binding of the substrates with an ordered kinetic mechanism in which ligand binding inevitably closes the active site. In this work, we challenge this assumption by reporting the crystal structures of intermediate forms of MurD either in the absence of ligands or in the presence of small molecules. A detailed analysis provides insight into the events that lead to the closure of MurD and reveals that minor structural modifications contribute to major overall conformation alterations. These novel insights will be instrumental in the development of new potential antibiotics designed to target the peptidoglycan biosynthetic pathway.
Topics: Crystallography, X-Ray; Escherichia coli; Peptide Synthases; Peptidoglycan; Protein Structure, Tertiary
PubMed: 27031227
DOI: 10.1371/journal.pone.0152075 -
International Journal of Molecular... May 2021One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND)...
One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND) transporters are highly studied, as being responsible for one of the most problematic mechanisms used by bacteria to resist to antibiotics, i.e., the active efflux of drugs. In Gram-negative bacteria, these proteins are inserted in the inner membrane and form a tripartite assembly with an outer membrane factor and a periplasmic linker in order to cross the two membranes to expulse molecules outside of the cell. A lot of information has been collected to understand the functional mechanism of these pumps, especially with AcrAB-TolC from , but one missing piece from all the suggested models is the role of peptidoglycan in the assembly. Here, by pull-down experiments with purified peptidoglycans, we precise the MexAB-OprM interaction with the peptidoglycan from and , highlighting a role of the peptidoglycan in stabilizing the MexA-OprM complex and also differences between the two Gram-negative bacteria peptidoglycans.
Topics: Bacterial Outer Membrane Proteins; Cell Wall; Drug Resistance, Bacterial; Escherichia coli; Membrane Transport Proteins; Models, Molecular; Peptidoglycan; Protein Interaction Domains and Motifs; Protein Stability; Protein Structure, Quaternary; Pseudomonas aeruginosa
PubMed: 34070225
DOI: 10.3390/ijms22105328 -
Chemistry & Biology May 2008Peptidoglycan (PGN) is a unique and essential structural part of the bacterial cell wall. PGNs from two contrasting Gram-negative plant pathogenic bacteria elicited...
Peptidoglycan (PGN) is a unique and essential structural part of the bacterial cell wall. PGNs from two contrasting Gram-negative plant pathogenic bacteria elicited components characteristic of the innate immune system in Arabidopsis thaliana, such as transcription of the defense gene PR1, oxidative burst, medium alkalinization, and formation of callose. Highly purified muropeptides from PGNs were more effective elicitors of early defense responses than native PGN. Therefore, PGN and its constituents represent a Microbe-Associated Molecular Pattern (MAMP) in plant-bacterial interactions. PGN and muropeptides from aggressive Xanthomonas campestris pv. campestris were significantly more active than those from Agrobacterium tumefaciens, which must maintain host cell viability during infection. The structure of muropeptide components and the distinctive differences are described. Differing defense-eliciting abilities appear to depend on subtle structural differences in either carbohydrate or peptide groups.
Topics: Calcium; Chromatography, High Pressure Liquid; Gas Chromatography-Mass Spectrometry; Genes, Plant; Immunity, Innate; Mass Spectrometry; Nuclear Magnetic Resonance, Biomolecular; Peptides; Peptidoglycan; Plants; Rhizobium; Structure-Activity Relationship; Xanthomonas
PubMed: 18482696
DOI: 10.1016/j.chembiol.2008.03.017 -
Experientia Oct 1992Degradation products of peptidoglycan, the universal bacterial cell wall constituent, were previously found in animal tissues and urine. Reassessment and quantitative... (Review)
Review
Degradation products of peptidoglycan, the universal bacterial cell wall constituent, were previously found in animal tissues and urine. Reassessment and quantitative analysis of available data lead to an original concept, i.e. that eukaryotic cells synthesize peptidoglycan. We present a model in which this endogenously synthesized peptidoglycan is essential for the processes of eukaryotic cell division and sleep induction in animals. Genes for peptidoglycan metabolism, like those for lysine biosynthesis in plants, are probably inherited from endosymbiotic bacteria, the ancestors of mitochondria and chloroplasts. Corollaries of this concept, i.e. roles for peptidoglycan metabolism in tumor formation and in the biological clock, are supported by abundant evidence. We propose that many interactions between bacteria and eukaryotes are conditioned by their common genetic heritage.
Topics: Animals; Bacteria; Carbohydrate Sequence; Humans; Molecular Sequence Data; Peptidoglycan; Periodicity; Phylogeny; Plants
PubMed: 1426143
DOI: 10.1007/BF01919139 -
PLoS Computational Biology Feb 2014Bacteria face the challenging requirement to maintain their shape and avoid rupture due to the high internal turgor pressure, but simultaneously permit the import and...
Bacteria face the challenging requirement to maintain their shape and avoid rupture due to the high internal turgor pressure, but simultaneously permit the import and export of nutrients, chemical signals, and virulence factors. The bacterial cell wall, a mesh-like structure composed of cross-linked strands of peptidoglycan, fulfills both needs by being semi-rigid, yet sufficiently porous to allow diffusion through it. How the mechanical properties of the cell wall are determined by the molecular features and the spatial arrangement of the relatively thin strands in the larger cellular-scale structure is not known. To examine this issue, we have developed and simulated atomic-scale models of Escherichia coli cell walls in a disordered circumferential arrangement. The cell-wall models are found to possess an anisotropic elasticity, as known experimentally, arising from the orthogonal orientation of the glycan strands and of the peptide cross-links. Other features such as thickness, pore size, and disorder are also found to generally agree with experiments, further supporting the disordered circumferential model of peptidoglycan. The validated constructs illustrate how mesoscopic structure and behavior emerge naturally from the underlying atomic-scale properties and, furthermore, demonstrate the ability of all-atom simulations to reproduce a range of macroscopic observables for extended polymer meshes.
Topics: Biophysical Phenomena; Cell Wall; Computational Biology; Computer Simulation; Escherichia coli; Models, Molecular; Molecular Conformation; Molecular Dynamics Simulation; Molecular Structure; Peptidoglycan
PubMed: 24586129
DOI: 10.1371/journal.pcbi.1003475 -
Lancet (London, England)
Topics: Bacillus; Dialysis Solutions; Drug Contamination; Glucans; Glucose; Humans; Icodextrin; Peptidoglycan; Peritoneal Dialysis; Peritonitis
PubMed: 16039325
DOI: 10.1016/S0140-6736(05)66976-0 -
Journal of Bacteriology Jan 1991Fusobacterium nucleatum was grown in the presence of [14C]UDP. By means of sequential precipitation and chromatographic separation of the cytoplasmic content, a...
Fusobacterium nucleatum was grown in the presence of [14C]UDP. By means of sequential precipitation and chromatographic separation of the cytoplasmic content, a peptidoglycan [14C]UDP pentapeptide containing lanthionine was isolated. This finding indicates that lanthionine is synthesized and incorporated as such during the assembly of the peptidoglycan.
Topics: Alanine; Carbon Radioisotopes; Chromatography, Gel; Chromatography, High Pressure Liquid; Fusobacterium; Peptidoglycan; Sulfides; Uridine Diphosphate
PubMed: 1987169
DOI: 10.1128/jb.173.2.900-902.1991 -
Annual Review of Cell and Developmental... 1997Bacteria usually divide by building a central septum across the middle of the cell. This review focuses on recent results indicating that the tubulin-like FtsZ protein... (Review)
Review
Bacteria usually divide by building a central septum across the middle of the cell. This review focuses on recent results indicating that the tubulin-like FtsZ protein plays a central role in cytokinesis as a major component of a contractile cytoskeleton. Assembly of this cytoskeletal element abutting the membrane is a key point for regulation. The characterization of FtsZ homologues in Mycoplasmas, Archaea, and chloroplasts implies that the constriction mechanism is conserved and that FtsZ can constrict in the absence of peptidoglycan synthesis. In most Eubacteria, the internal cytoskeleton must also regulate synthesis of septal peptidoglycan. The Escherichia coli septum-specific penicillin-binding protein 3 (PBP3) forms a complex with other enzymes involved in murein metabolism, suggesting a centrally located transmembrane complex capable of splicing multiple new strands of peptidoglycan into the cell wall. Important questions remain about the spatial and temporal control of bacterial division.
Topics: Bacteria; Bacterial Proteins; Cell Cycle; Cell Division; Cytoskeletal Proteins; Cytoskeleton; Peptidoglycan
PubMed: 9442879
DOI: 10.1146/annurev.cellbio.13.1.395 -
Methods in Enzymology 2002
Topics: Bacterial Proteins; Cell Membrane; Chromatography, High Pressure Liquid; Indicators and Reagents; Peptidoglycan; Salmonella; Salmonella typhimurium; Solubility; Virulence
PubMed: 12474403
DOI: 10.1016/s0076-6879(02)58105-2