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ATP synthase is a universal molecular machine for energy conversion. By coupling to cellular respiration in mitochondria, it catalyzes conversion of chemical energy of cells.
Mitochondrial ATP synthase is composed of dimers that, when come together, form membrane curvature that is essential for efficient energy conversion. While the mitochondrial signature lipid cardiolipin and its interactions with proteins are believed to contribute to this process, it was not directly visualized before. In addition, it was unclear to what extent the ATP synthase has diverged across different species.
Alexander - Mühleip - Amunts - Lab - Organism
Alexander Mühleip from Amunts lab used the single-cell photosynthetic organism Euglena gracilis, which belongs to a phylum that also includes human parasites, to extract the mitochondrial ATP synthase. Its structure was then determined using cryo-EM, allowing the reconstruction of the atomic model. The high resolution of the cryo-EM density map allowed identification of 29 different protein subunits and 25 cardiolipin molecules. Some of the cardiolipins appear to modulate the critical channel for proton transfer that fuels the...
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