An electron transfer path connects subunits of a mycobacterial respiratory supercomplex
| Autor: | Minze Jia, Luke W. Guddat, Lu Yu, Guanghou Shui, Shuhui Wang, Wenxin Ji, Zhiyong Lou, Ao Xu, Ruogu Gao, Hongri Gong, Hsin-Yung Yen, Jingwen Li, Biao Jiang, Fei Sun, Jun Li, Carol V. Robinson, Zihe Rao, Changlin Tian, Luet-Lok Wong, Quan Wang, Xuemei Li, Sin Man Lam, Xiuna Yang, Cheng Yang, Yuna Sun, Yanting Tang |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Cytochrome Stereochemistry Protein subunit Mycobacterium smegmatis 030106 microbiology Oxidative Phosphorylation Electron Transport Electron Transport Complex IV Electron Transport Complex III 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Cytochrome c oxidase Multidisciplinary biology Superoxide Dismutase Chemistry Superoxide Cryoelectron Microscopy Periplasmic space biology.organism_classification Electron transport chain Actinobacteria Oxygen 030104 developmental biology Coenzyme Q – cytochrome c reductase biology.protein Protein Multimerization Oxidation-Reduction |
| Popis: | We report a 3.5-angstrom-resolution cryo–electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis. |
| Databáze: | OpenAIRE |
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