Fig. 2: Superposition of models in IF or OF conformations.
From: Rhodamine6G and Hœchst33342 narrow BmrA conformational spectrum for a more efficient use of ATP
Colors match the ones of Fig. 1 and Supplementary Fig. 9. Protein in cartoon and ligands are in sticks, TM helices are numbered when appropriate. A–C BmrA in the IF conformation seen from the side, from under the NBD or a close-up view of the substrate-binding pocket, respectively (E504Aapo in blue, E504AR6G in red, E504A25µMATP in skyblue, E504A100µMATP in lightblue, E504AR6G-25µMATP in salmon). Overlay was performed on the 3 first TM helices of chain A, residues 1-161. On (B), a line is drawn between residues 577 of each monomer to highlight the conformational change. D, E show BmrA in the OF conformation (E504A100µMATP in lightblue, E504A5mMATP in gray, E504AR6G-70µMATP in yellow, E504AR6G-5mMATP in green), with (E) being a close-up view of the TM1-2 loop with R6G in its pocket. Overlay was performed on the last 4 helices of chain A, residues 104-300 as in ref. 12. F–H BmrA in the IF conformation in complex with Hœchst33342 (E504AH33342) seen from the side, from under the NBD or a close-up view of the substrate-binding pocket, respectively. E504AH33342 is colored in green cartoon and Hœchst33342 is shown as spheres in (F) and as sticks in (H) colored by atom type with carbons in green. E504AH33342 is overlaid with E504Aapo (blue) in residues 1-161 of chain A in (F–H), and shown with the structures complexed with R6G (E504AR6G in red) in (H) to asses ligand positioning. Chemical structures of R6G and Hœchst33342 are shown in the picture.
