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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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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0005-622C-C Versions-Permalink: https://hdl.handle.net/21.11116/0000-000C-D284-1
Genre: Zeitschriftenartikel

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 Urheber:
Parey, Kristian1, 2, 3, Autor           
Haapanen, Outi4, Autor
Sharma, Vivek4, 5, Autor
Köfeler, Harald6, Autor
Züllig, Thomas6, Autor
Prinz, Simone1, 7, Autor           
Siegmund, Karin2, 3, Autor
Wittig, Ilka8, Autor
Mills, Deryck1, Autor                 
Vonck, Janet1, Autor                 
Kühlbrandt, Werner1, Autor                 
Zickermann, Volker2, 3, Autor
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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 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2019-05-072019-10-222019-12-11
 Publikationsstatus: Online veröffentlicht
 Seiten: 11
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1126/sciadv.aax9484
BibTex Citekey: parey_high-resolution_2019
 Art des Abschluß: -

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Titel: Science Advances
  Andere : Sci. Adv.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington : AAAS
Seiten: - Band / Heft: 5 (12) Artikelnummer: - Start- / Endseite: eaax9484 Identifikator: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548