Science (American Association for the Advancement of Science), 2018-11, Vol.362 (6418)
2018
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- An electron transfer path connects subunits of a mycobacterial respiratory supercomplex
- Ist Teil von
- Science (American Association for the Advancement of Science), 2018-11, Vol.362 (6418)
- Ort / Verlag
- United States: The American Association for the Advancement of Science
- Erscheinungsjahr
- 2018
- Quelle
- Science Online_科学在线
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.aat8923Titel-ID: cdi_proquest_miscellaneous_2126907845
- Format
- –
- Schlagworte
- Actinobacteria - enzymology, Bacteria, Bacterial Proteins - chemistry, Binding sites, Cofactors, Corynebacterium glutamicum, Cryoelectron Microscopy, Cytochrome, Cytochrome c, Cytochromes, Detoxification, Dimers, Domains, Drug discovery, Electron microscopy, Electron transfer, Electron Transport, Electron transport chain, Electron Transport Complex III - chemistry, Electron Transport Complex IV - chemistry, Electron tunneling, Gram-negative bacteria, Gram-positive bacteria, Hydroquinone, Immune response, Macromolecules, Macrophages, Metabolism, Microscopy, Mitochondria, Molecular structure, Monomers, Mycobacterium smegmatis, Mycobacterium smegmatis - enzymology, Mycobacterium tuberculosis, Oxidation, Oxidation resistance, Oxidation-Reduction, Oxidative Phosphorylation, Oxidative stress, Oxygen, Oxygen - metabolism, Protein Multimerization, Proteins, Protons, Quinones, Reduction, Respiration, Spacecraft components, Superoxide dismutase, Superoxide Dismutase - chemistry, Transmission electron microscopy, Tuberculosis