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ATP synthase produces the majority of cellular energy in most cells. We have previously reported cryo-EM maps of autoinhibited  E. coli  ATP synthase imaged without addition of nucleotide (Sobti et al. 2016), indicating that the subunit ε engages the α, β and γ subunits to lock the enzyme and prevent functional rotation. Here we present multiple cryo-EM reconstructions of the enzyme frozen after the addition of MgATP to identify the changes that occur when this ε inhibition is removed. The maps generated show that, after exposure to MgATP,  E. coli  ATP synthase adopts a different conformation with a catalytic subunit changing conformation substantially and the ε C-terminal domain transitioning via an intermediate ‘half-up’ state to a condensed ‘down’ state. This work provides direct evidence for unique conformational states that occur in  E. coli  ATP synthase when ATP binding prevents the ε C-terminal domain from entering the inhibitory ‘up’ state.

Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP