Figure 5 - full size

 

Figure 5.
Fig. 5. The transition state of the IIA^Mtl-P-HPr complex. A, detailed view around the active site histidines, illustrating the backbone and side chain positions in the unphosphorylated complex, the dissociative transition state, and the associative transition state. The backbones of IIA^Mtl and HPr are shown in dark blue and dark green, respectively, for the unphosphorylated complex, and in light blue and light green, respectively, for the putative dissociative and associative transition states; the active site histidines and pentacoordinate phosphoryl group (in the case of the transition states) are shown in purple for the unphosphorylated complex, in red for the dissociative transition state (N 2-N 1 distance of ~6 Å between His-65 and His-15), and in orange for the associative transition state (N 2-N 1 distance of ~4 Å between His-65 and His-15). Small changes in the backbone of residues 64-66 of IIA^Mtl and residues 14-16 of HPr are required to accommodate the transition states. B, detailed view of the active site in the putative transition state illustrating the interactions that stabilize the phosphoryl group. The color coding is as follows: the backbone and side chains of IIA^Mtl are shown in blue and red, respectively; the backbone and side chains of HPr are shown in green and gray, respectively; the active site histidines are in purple, and the pentacoordinate phosphoryl group is in yellow. Residues from HPr are labeled in italics.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 42289-42298) copyright 2002.