BSB Seminar: How ATP synthase works

Alastair Stewart, Victor Chang Cardiac Research Institute


F1Fo ATP synthase generates the majority of cellular energy by interconverting phosphate transfer energy and proton motive force via a rotary catalytic mechanism. Using cryo electron microscopy we have provided molecular snapshots of this complex enzyme in multiple states. Combining this data with single molecule recordings, mutagenesis and mass spectrometry has generated a detailed picture of how this essential biological motor functions.


Alastair is a laboratory head at the Victor Chang Cardiac Research Institute in Sydney Australia. Throughout his career he has used a complementary spectrum of structural and biochemical methods to elucidate the function of large protein complexes. Alastair read the Natural Sciences Tripos at the University of Cambridge before moving to Sydney Australia to work with Dr Daniela Stock. After gaining laboratory skills he embarked on a PhD to understand the function of T. thermophilus A-type ATPase, showing how it is flexibly coupled. He then performed a short postdoc investigating how long non-coding RNAs regulate histone modifications, before setting up his independent research group at the Victor Chang Cardiac Research Institute in 2016 with a fellowship from the National Health and Medical Research Council. Since then, he has been driven to understand the function and substrate specificity of a range of macromolecules including ATP synthases, chaperonins, drug transporters and ion channels.