Figure 5
Computational studies of the structural model for the complex Myr-sortase A (SrtA). (a) Overall fold of SrtA highlighting regions undergoing large substrate-induced conformational changes. (b) Detail of the LPXTG sequence analog covalently bound to SrtA. (c) Lowest energy conformation of Myr representative of the lowest energy and most populated conformational cluster obtained through molecular docking calculations. Receptor residues are represented in gray and ligands in cyan. Potential hydrogen-bond interactions are shown in dashed black lines. Methodology can be found in Supplementary Methods.
