Fig. 5

Local conformational rearrangements within the C domain induced by the effectors binding in a synergistic manner. Effector-site superposition of five MtbPYK structures in different ligand-bound states showing the structural rearrangements of the synergistic mechanism. The polypeptide chains are shown as cartoons, while interacting residues are shown as sticks. The carbon atoms of the effectors AMP and G6P are represented by grey sticks. The movements of α helixes (Cα1, Cα4 and Aα6′–Aα6) and the flip of the side chain of Trp398 are indicated by arrows. Interactions between MtbPYK and the effectors are shown as dashed lines, together with the corresponding distances. The relative locations of the five implicated α helixes within a subunit are shown in the inset (i) where the active site, allosteric effector-binding site and domains are indicated. The α helixes Cα3 and Aα6′–Aα6 are shown as green and red, respectively. The distance between the active site and effector is about 40 Å