Fig. 3: Structures of LspMrs in complex with globomycin and with myxovirescin.

a, b Views from the membrane into the binding pocket containing globomycin and myxovirescin, respectively. c Detailed view of the blocking hydroxy group (6-OH) of myxovirescin interacting with the catalytic aspartate residues. d–f Comparison of myxovirescin and globomycin in the binding pocket of LspMrs. Superposed protein structures are shown in the background with parts removed for clarity. Catalytic aspartate dyad residues are shown with carbons in dark blue. A superpose of the two antibiotics in the binding pocket is shown in e. Because myxovirescin has a complicated bent ovoid shape (Supplementary Fig. 11) it is impossible to find a single orientation where all of its non-hydrogen atoms are visible. For a fuller appreciation of myxovirescin’s molecular shape, the reader is referred to the Protein Data Bank record (PDB ID, 6RYP). In b, the C-terminal residues K¹⁵⁷, K¹⁵⁸, E¹⁵⁹, K¹⁶⁰, E¹⁶¹, V ¹⁶² and K¹⁶³, which extend into the cytoplasm as a helix/coil, have been deleted for a more uniform comparison with a where these residues are disordered. Distances are shown in ångströms as dashed lines.