Molecular mechanism of rotary ATPases and their role as new targets in infectious diseases

ATP is the universal energy storage molecule living cells use to power biochemical reactions. A human being needs approximately their own body weight of ATP per day. ATP is produced by the enzyme ATP synthase; it converts the energy stored in an electro-chemical gradient of protons or sodium ions into ATP and operates by a unique rotary mechanism. Professor Meier aims to understand the structure and operation principles of this molecular machine, and to decipher its mechanism using structural and biophysical methods, including cryo-EM and X-ray crystallography. Specifically, he will investigate how rotary ATPases dynamically couple ion translocation with ATP synthesis and how new types of drugs and inhibitors, such as the class of diarylquinolines, attack and inhibit rotary ATPases on a molecular level.