An electron transfer path connects subunits of a mycobacterial respiratory supercomplex
We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from 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 t...
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| Published in: | Science (American Association for the Advancement of Science) Vol. 362; no. 6418 |
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| Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
United States
30.11.2018
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| Subjects: | |
| ISSN: | 1095-9203, 1095-9203 |
| Online Access: | Get more information |
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| Summary: | We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from
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. |
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| Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ISSN: | 1095-9203 1095-9203 |
| DOI: | 10.1126/science.aat8923 |