Abstract
The novel antibiotic compound teixobactin showed bactericidal capabilities against Gram-positive bacteria by sequestering cell-wall biosynthesis precursors. We have previously modeled the membrane-bound teixobactin/lipid II complex using MD simulations and concluded that the binding centers around teixobactin's C-terminal cyclodepsipeptide ring. Recently, the lipid II-bound structure of a highly active teixobactin derivative (R4L10-teixobactin) in a membrane environment was determined using ssNMR.
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