Fig. 6
Comparison between ΔG7048 and RmBgt17A. a Structural-based sequence alignment between ΔG7048 and RmBgt17A. Identical residues are shown on a red background and conservatively mutated residues are shown in red on white background. The catalytic residues, E111 and E222, are marked with blue dots. Residues reported to be involved in direct or H2O-mediated interaction with the substrate in RmBgt17A are underlined in green and orange, respectively. Residues limiting the access to the catalytic cleft in RmBgt17A are underlined in black. Regions corresponding to the 4 sites described in panel b are indicated by black boxes. The sequences were aligned by Chimera and the figure was produced in ESPript. b Structural superposition of ΔG7048 (blue) with the ligand free form of RmBgt17A (PDB: 4wtp, pink). c structural superposition of ΔG7048 (blue) with (i) ligand free RmBgt17A (PDB: 4wtp, pink), (ii) LAM2-RmBgt17A (PDB: 4wtr, green) and (iii) LAM3-RmBgt17A (PDB: 4wts, yellow). d Surface representation of ΔG7048 (left) and RmBgt17A (PDB: 4wtp, right) with substrates from RmBgt17A structures (PDB: 4wtr, PDB: 4wts) located in the catalytic cleft without further docking experiment or energy minimization procedure. e Close view of the substrate binding region of structures superposed in c. Catalytic residues and those directly contacting the substrates in RmBgt17A with the corresponding ones in ΔG7048 are representing in sticks (numbering according to the ΔG7048 sequence)