| Literature DB >> 30361386 |
Hongri Gong1, Jun Li2,3, Ao Xu1,4, Yanting Tang1, Wenxin Ji4,5, Ruogu Gao4,5, Shuhui Wang2,3, Lu Yu6, Changlin Tian6,7, Jingwen Li8, Hsin-Yung Yen8,9, Sin Man Lam10, Guanghou Shui10, Xiuna Yang2,3, Yuna Sun4, Xuemei Li4, Minze Jia4, Cheng Yang1, Biao Jiang2, Zhiyong Lou11, Carol V Robinson8, Luet-Lok Wong12, Luke W Guddat13, Fei Sun14,5, Quan Wang14, Zihe Rao15,2,3,4,11.
Abstract
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.Entities:
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Year: 2018 PMID： 30361386 DOI： 10.1126/science.aat8923
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728