| Structural highlights
Function
A0R057_MYCS2
Publication Abstract from PubMed
We report a 3.5-A resolution cryo-EM 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 such that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV via a bridging cytochrome subunit. We observe 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 development of treatments for human tuberculosis.
An electron transfer path connects subunits of a mycobacterial respiratory supercomplex.,Gong H, Li J, Xu A, Tang Y, Ji W, Gao R, Wang S, Yu L, Tian C, Li J, Yen HY, Man Lam S, Shui G, Yang X, Sun Y, Li X, Jia M, Yang C, Jiang B, Lou Z, Robinson CV, Wong LL, Guddat LW, Sun F, Wang Q, Rao Z Science. 2018 Oct 25. pii: science.aat8923. doi: 10.1126/science.aat8923. PMID:30361386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gong H, Li J, Xu A, Tang Y, Ji W, Gao R, Wang S, Yu L, Tian C, Li J, Yen HY, Man Lam S, Shui G, Yang X, Sun Y, Li X, Jia M, Yang C, Jiang B, Lou Z, Robinson CV, Wong LL, Guddat LW, Sun F, Wang Q, Rao Z. An electron transfer path connects subunits of a mycobacterial respiratory supercomplex. Science. 2018 Oct 25. pii: science.aat8923. doi: 10.1126/science.aat8923. PMID:30361386 doi:http://dx.doi.org/10.1126/science.aat8923
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