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High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease

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Parey,  Kristian
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biochemistry II, University Hospital, Goethe University, Frankfurt am Main, Germany;
Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Frankfurt am Main, Germany;

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Prinz,  Simone
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society;

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Mills,  Deryck       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Vonck,  Janet       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Parey, K., Haapanen, O., Sharma, V., Köfeler, H., Züllig, T., Prinz, S., et al. (2019). High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease. Science Advances, 5(12), eaax9484. doi:10.1126/sciadv.aax9484.


Cite as: https://hdl.handle.net/21.11116/0000-0005-622C-C
Abstract
Respiratory complex I is a redox-driven proton pump, accounting for a large part of the electrochemical gradient that powers mitochondrial adenosine triphosphate synthesis. Complex I dysfunction is associated with severe human diseases. Assembly of the one-megadalton complex I in the inner mitochondrial membrane requires assembly factors and chaperones. We have determined the structure of complex I from the aerobic yeast Yarrowia lipolytica by electron cryo-microscopy at 3.2-Å resolution. A ubiquinone molecule was identified in the access path to the active site. The electron cryo-microscopy structure indicated an unusual lipid-protein arrangement at the junction of membrane and matrix arms that was confirmed by molecular simulations. The structure of a complex I mutant and an assembly intermediate provide detailed molecular insights into the cause of a hereditary complex I-linked disease and complex I assembly in the inner mitochondrial membrane.