Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1

Abstract

ATP production under lockdown Cellular processes must respond to change, often by speeding up, slowing down, or stopping altogether. Adenosine triphosphate (ATP) synthases use a transmembrane proton gradient to produce ATP, but this reaction can go in reverse and needs to be halted when conditions are unfavorable. Jinke Gu et al. purified a tetrameric ATP synthase complex from pig hearts that contained the endogenous inhibitory protein IF1. Targeted refinement yielded high-resolution views of the mammalian ATP synthase trapped in two different rotation states by IF1. The findings suggest that ATP synthase tetramers can be inhibited by at least three different mechanisms. Science , this issue p. 1068