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Structure of a complete yeast ATP synthase dimer shows molecular basis of inner mitochondrial membrane morphology

August 2016. Mitochondrial F1Fo-ATP synthase produces most ATP in cell by rotary catalysis. Rows of ATP synthase dimers are a prerequisite for the formation of inner membrane cristae, a hallmark signature of mitochondrial morphology. Cristae formation extends the membrane surface to accommodate a large number of respiratory chain complexes, making it possible to meet the high energy demands of eukaryotic cells. They also form a mitochondrial sub-compartment that supports a locally increased proton concentration in the confined cristae space. The complete structure of a yeast mitochondrial ATP synthase dimer published this month in the journal Molecular Cell offers important new insights into how mitochondria became the efficient power plants of eukaryotic cells.

Yeast ATP synthases have a subunit composition very similar to that of mammals and form the same V-shaped dimers. By a combination of cryo-electron microscopy and X-ray crystallography, a team of scientists from the Max Planck Institute of Biophysics, Goethe University Frankfurt and Imperial College London have obtained the structure of the complete ATP synthase dimer from the aerobic yeast Yarrowia lipolytica. The combined maps resolve 58 of the 60 known protein subunits. The structure reveals the previously unknown subunit architecture of the dimer interface in the membrane, thereby providing major insights into mitochondrial membrane architecture.

Bacterial and chloroplast ATP synthases are comparatively simple and consist of only eight or nine different subunits, which are sufficient for ATP production. The chloroplast ATP synthase is monomeric  and no ATP synthase dimers have been reported in bacteria. By contrast, all known mitochondrial ATP synthases form dimers in the membrane that self-assemble into rows. Mitochondrial ATP synthases of yeasts and metazoans have eight more subunits, the structure and function of which had not been known. The new study shows how the mitochondria-specific subunits in the mitochondrial Fo subcomplex are arranged and what their function is. More ...


Werner Kühlbrandt
Max Planck Institute of Biophysics
Frankfurt am Main


Hahn A, Parey K, Bublitz M, Mills Deryck J, Zickermann V, Vonck J, Kühlbrandt W, Meier T (2016) Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology. Mol Cell 63:445-456 http:/dx.doi.org/10.1016/j.molcel.2016.05.037