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

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.

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 Creators:
Parey, Kristian1, 2, 3, Author           
Haapanen, Outi4, Author
Sharma, Vivek4, 5, Author
Köfeler, Harald6, Author
Züllig, Thomas6, Author
Prinz, Simone1, 7, Author           
Siegmund, Karin2, 3, Author
Wittig, Ilka8, Author
Mills, Deryck1, Author           
Vonck, Janet1, Author           
Kühlbrandt, Werner1, Author           
Zickermann, Volker2, 3, Author
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Institute of Biochemistry II, University Hospital, Goethe University, Frankfurt am Main, Germany, ou_persistent22              
3Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Frankfurt am Main, Germany, ou_persistent22              
4Department of Physics, University of Helsinki, Helsinki, Finland, ou_persistent22              
5Institute of Biotechnology, University of Helsinki, Helsinki, Finland, ou_persistent22              
6Core Facility Mass Spectrometry, Medical University of Graz, Graz, Austria, ou_persistent22              
7Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              
8Functional Proteomics, SFB815 Core Unit, Medical School, Goethe University, Frankfurt am Main, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2019-05-072019-10-222019-12-11
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/sciadv.aax9484
BibTex Citekey: parey_high-resolution_2019
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Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 5 (12) Sequence Number: - Start / End Page: eaax9484 Identifier: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548