Figure 4
Schematic view of protein-protein interactions on the three-fold axis (A) and on the four-fold axis (C) (see Table 2 for details). (B) Close up view of the region around the three-fold axis. W67 forms a T-shaped van der Waals interaction with the adjacent homologs; this is the only point where a monomer interacts with two neighbours. The hydrophobic contact area of residues W67, L63, F61 and L56 defines a “hot-spot” motif in which binding energy is largely concentrated. (D) View from the interior along the C 4 axis; the mobile gate moieties are coloured red to emphasise the steric hindrance is interfering with the release of α-Tol.
