Structure of complete ATP synthase and its role as a new drug target against tuberculosis
F1Fo-ATP synthases are paradigmatic molecular machines, which use the transmembrane electrochemical ion gradient to power ATP synthesis. The enzymes belong to the class of rotary ATPases, which all share a common architecture, consisting of a rotor and stator entity. While ions are shuttled through the Fo complex of the enzyme, torque is generated at the rotor/stator and transferred to the F1-catalytic subunits for ATP synthesis. In the opposite direction, ATP hydrolysis can be used to drive ion pumping. In my talk I will present the structure of the complete ATP synthase analysed by electron cryo-microscopy and X-ray crystallography. I will also focus on biochemical and structural investigations of the ATP synthase with respect to the development of new antibiotics in the fight against infectious diseases such as tuberculosis.