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SHR Neuro Krebs Kardio Lipid Stoffw Microb

Parey, K; Haapanen, O; Sharma, V; Köfeler, H; Züllig, T; Prinz, S; Siegmund, K; Wittig, I; Mills, DJ; Vonck, J; Kühlbrandt, W; Zickermann, V.
High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease.
Sci Adv. 2019; 5(12): eaax9484-eaax9484. Doi: 10.1126/sciadv.aax9484 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG

 

Co-Autor*innen der Med Uni Graz
Köfeler Harald
Züllig Thomas
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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. Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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