Fig. 2: Lipid II binding interface.
a, Chemical structure of lipid II. b, 1D 31P ssNMR data show strong shifts of the lipid II pyrophosphate signals upon binding of plectasin. c, 13C-31P ssNMR REDOR16 data show slower decay of the pyrophosphate signals in the 13C-plectasin–lipid II complex compared to the 13C-teixobactin–lipid II complex. This implies that the interaction between PPi and plectasin is more dynamic. The reported error is one unit of standard deviation, calculated on the Sr/S0 ratio on the bases of the experimental errors in the integrated spectra. Source data are provided. d, Cartoon representation of plectasin showing the presumed residues that interact with lipid II. e, Overlay of 2D ssNMR 13C13C PARISxy45 spectra of plectasin in complex with NMR-visible 13C,15N-labelled lipid II (in cyan) and NMR-invisible 12C,14N lipid II (in yellow and grey) with different CC mixing times that show contacts between aromatic residues (Y25, Y29, Y40) of plectasin and lipid II sugars. LII, lipid II. f, A combination of scalar17 (that show only mobile residues) and dipolar (that show only rigid residues) 2D CC ssNMR spectra show that the pentapeptide is more flexible in the teixobactin–lipid II complex than in the plectasin–lipid II complex. Upper panel: overlay of scalar (in orange) and dipolar (in blue) ssNMR spectra of the pentapeptide in the plectasin–lipid II complex. Lower panel: overlay of scalar ssNMR spectra of the pentapeptide in complex with plectasin (in orange) and teixobactin (in green). g, Cartoon representations of the plectasin–lipid II and teixobactin–lipid II complexes.
