Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase

This is the authors' abstract. We don't add key points for this paper.

Innovations in an ATPase/ATP synthase Enzymes that couple the chemical energy of adenosine triphosphate (ATP) to movement of ions across a membrane are present in all domains of life. Like their F-type cousins in mitochondria, chloroplasts, and most bacteria, vacuolar/archaeal (V/A-type) ATPases couple synthesis or hydrolysis of ATP to movement of protons across the membrane. To uncover mechanistic differences in energy coupling between F- and V/A-type enzymes, Zhou and Sazanov determined structures of a V/A-type ATP synthase from the bacterium Thermus thermophilus. With structures of multiple substates visible, the domain interfaces are made clear and a role for the elastic peripheral stalks is apparent in coupling rotational energy from V o into the ATP-synthesizing V 1 domain. Science , this issue p. eaaw9144