ATP Synthase: The Right Size Base Model for Nanomotors in Nanomedicine
Figure 2
Catalytic sites X-ray structure of ATP synthase depicting spatial relationship between and -subunit residues. The DP site in the -inhibited enzyme structure is taken from [63]. E. coli residue numbering is used. It can be seen that removal of arginine from R246 can be compensated by introduction of arginine in the neighboring residues F291 or N243. Dotted triangle shows the residues Lys-155, Arg-182, Arg-246, Arg-376, and Ser-347, forming a triangular Pi binding site. Figure was modified from the originally published figure in [75]. RasMol molecular visualization software was used to generate the figure.
