Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria
Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria
Significance The structure of mitochondrial cristae in different species and tissues is highly variable. The molecular basis of these variations and their effect on mitochondrial function is not understood. Dimers of ATP synthase, the essential membrane protein complex that produces most of the ATP in the cell, are thought to shape lamellar cristae, for example in humans or yeasts. Here, we present the ATP synthase dimer structure from the ciliate Paramecium tetraurelia, which assembles into helical arrays around the outer perimeter of twisted tubular cristae. The similarities between the morphology of the helical arrays and the tubular cristae indicate that ATP synthase dimers are responsible for shaping the cristae of mitochondria.
- University of California, San Francisco United States
- Goethe University Frankfurt Germany
- Max Planck Institute of Biophysics Germany
- Max Planck Society Germany
Models, Molecular, Microscopy, Protein Structure, Secondary, serial block face imaging, Paramecium, Protein Conformation, macromolecular organization, cryoelectron microscopy, Protozoan Proteins, Molecular, Mitochondrial Proton-Translocating ATPases, Electron, Protein Structure, Secondary, Mitochondria, Microscopy, Electron, Models, Mitochondrial Membranes, subtomogram averaging, Animals, Paramecium tetraurelia, Protein Multimerization
Models, Molecular, Microscopy, Protein Structure, Secondary, serial block face imaging, Paramecium, Protein Conformation, macromolecular organization, cryoelectron microscopy, Protozoan Proteins, Molecular, Mitochondrial Proton-Translocating ATPases, Electron, Protein Structure, Secondary, Mitochondria, Microscopy, Electron, Models, Mitochondrial Membranes, subtomogram averaging, Animals, Paramecium tetraurelia, Protein Multimerization
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