Figure 6 - full size

 

Figure 6.
Figure 6. Two conformations of the E151D monomer in stereo. The E151D monomer has an N-terminal dsDNA-binding domain (top) and a larger ATPase core domain (bottom). The ATPase domain has two half-sites for binding ATP (gold). Two putative DNA-binding regions L1 (green) and L2 (magenta and blue for the two observed conformations, respectively) are located near the filament axis (dotted vertical line). Both ends of the L2 region contact the ATP-binding site. Two K^+ (in yellow) were observed to form bridges between the γ–phosphate of AMP–PNP and the short helix in the L2 region (in magenta). When KCl was substituted for NaCl, the L2 region (in blue) became largely disordered.

The above figure is reprinted by permission from Elsevier: J Mol Biol (2006, 360, 537-547) copyright 2006.