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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.

Original publication

DOI

10.1126/science.aat8923

Type

Journal article

Journal

Science

Publication Date

30/11/2018

Volume

362

Keywords

Actinobacteria, Bacterial Proteins, Cryoelectron Microscopy, Electron Transport, Electron Transport Complex III, Electron Transport Complex IV, Mycobacterium smegmatis, Oxidation-Reduction, Oxidative Phosphorylation, Oxygen, Protein Multimerization, Superoxide Dismutase