Fig. 11.

Homology model of Mt-PrsA. (A) Mt-PrsA arranged into its hexameric quaternary conformation. Carbon atoms of the ADP ligands located at the catalytic and regulatory sites of the Mt-PrsA hexamer are colored in orange and green, respectively. Red spheres located at K10, D169, G194, D205-V208 and F322 indicate regions of the Mt-PrsA dimmer that include insertions or deletions with respect to the Bs-Prs structure. The triangle in the middle represents 3-fold symmetry, where as the arrow parallel to the plane indicates 2-fold rotational symmetry. Catalytic (B) and regulatory (C) sites of the Mt-PrsA homology model. The yellow and the blue spheres indicate A85/G88 and S109/G111 substitution between the Bs-Prs and Mt-PrsA structures, respectively.