Figure 6
From: Ligand-induced conformational changes in a thermophilic ribose-binding protein
Comparison of ligand-induced local conformational changes in the protein backbone of T. maritima and E. coli RBPs. The absolute value of the change in the dihedral angle determined by four successive Cα atoms is shown [41]. (A) Comparison between the A and B molecules of the T. maritima RBP apoprotein reveals that these two molecules differ primarily in the hinge region and represent different points along the hinge bending trajectory. (B) Comparison between molecule B of the apoprotein and the ribose-complexed tmRBP. (C) Comparison between molecule A of the apoprotein and the ribose-complexed tmRBP. (D) Comparison of the apo and ribose-complexed ecRBP (PDB code 1URP and 2DRI respectively). The span of the N- and C-terminal domains is indicated by solid horizontal lines; hinge regions are indicated by arrows. Regions near the binding pocket are marked by an asterisk. The mean of the |ΔCα| dihedral angle and one standard deviation away from the mean are indicated by a dashed and solid line respectively.