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Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic.
Resistance to antibiotics is increasing in some groups of clinically important pathogens. For instance, high vancomycin resistance has emerged in enterococci. Promising alternative antibiotics areExpand
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Specific Binding of Nisin to the Peptidoglycan Precursor Lipid II Combines Pore Formation and Inhibition of Cell Wall Biosynthesis for Potent Antibiotic Activity*
Unlike numerous pore-forming amphiphilic peptide antibiotics, the lantibiotic nisin is active in nanomolar concentrations, which results from its ability to use the lipid-bound cell wall precursorExpand
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The nisin–lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics
The emerging antibiotics-resistance problem has underlined the urgent need for novel antimicrobial agents. Lantibiotics (lanthionine-containing antibiotics) are promising candidates to alleviate thisExpand
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The C Terminus of SecA Is Involved in Both Lipid Binding and SecB Binding (*)
Using C-terminal deletion mutations in secA, we localized the previously proposed (Breukink, E., Keller, R. C. A., and de Kruijff, B.(1993), FEBS Lett. 331, 19-24) second lipid binding site on SecA.Expand
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Lipid II Is an Intrinsic Component of the Pore Induced by Nisin in Bacterial Membranes*
The peptidoglycan layers surrounding bacterial membranes are essential for bacterial cell survival and provide an important target for antibiotics. Many antibiotics have mechanisms of action thatExpand
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Lipid II as a target for antibiotics
Lipid II is a membrane-anchored cell-wall precursor that is essential for bacterial cell-wall biosynthesis. The effectiveness of targeting Lipid II as an antibacterial strategy is highlighted by theExpand
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An Alternative Bactericidal Mechanism of Action for Lantibiotic Peptides That Target Lipid II
Lantibiotics are polycyclic peptides containing unusual amino acids, which have binding specificity for bacterial cells, targeting the bacterial cell wall component lipid II to form pores and therebyExpand
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In Vitro Murein (Peptidoglycan) Synthesis by Dimers of the Bifunctional Transglycosylase-Transpeptidase PBP1B from Escherichia coli*
PBP1B is a major bifunctional murein (peptidoglycan) synthase catalyzing transglycosylation and transpeptidation reactions in Escherichia coli. PBP1B has been shown to form dimers in vivo. The KDExpand
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The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane.
The interaction of nisin Z and a nisin Z mutant carrying a negative charge in the C-terminus ([Glu-32]-nisin Z) with anionic lipids was characterized in model membrane systems, and bacterial membraneExpand
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The Essential Cell Division Protein FtsN Interacts with the Murein (Peptidoglycan) Synthase PBP1B in Escherichia coli*
Bacterial cell division requires the coordinated action of cell division proteins and murein (peptidoglycan) synthases. Interactions involving the essential cell division protein FtsN and mureinExpand
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