Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase
Figure 1
Escherichia coli ATP synthase structure: E. coli ATP synthase enzyme is composed of two sectors, water soluble F1 and membrane bound Fo. Catalytic activity occurs at the interface of αβ/subunits of F1 sector which consists of five subunits (α3β3γδε) and proton conduction occurs at the Fo sector consisting of three subunits (ab2c). One of the catalytic binding sites is identified with circle at the interface of α/β subunits. This model of E. coli ATP synthase is reproduced from Weber [6] with permission; copyright Elsevier.
