Science
Abstract
We report a 3.5-? 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.
论文编号: | DOI:10.1126/science.aat8923 |
论文题目: | An Electron Transfer Path Connects Subunits of a Mycobacterial Respiratory Supercomplex |
英文论文题目: | An Electron Transfer Path Connects Subunits of a Mycobacterial Respiratory Supercomplex |
第一作者: | Hongri Gong, Jun Li, Ao Xu, Yanting Tang, Wenxin Ji, Ruogu Gao, Shuhui Wang, Lu Yu, Changlin Tian, Jingwen Li, Hsin-Yung Yen, Sin Man Lam, Guanghou Shui, Xiuna Yang, Yuna Sun, Xuemei Li, Minze Jia, Cheng Yang, Biao Jiang, Zhiyong Lou, Carol V. Robinson, Luet-Lok Wong, Luke W. Guddat, Fei Sun, Quan Wang, Zihe Rao |
英文第一作者: | Hongri Gong, Jun Li, Ao Xu, Yanting Tang, Wenxin Ji, Ruogu Gao, Shuhui Wang, Lu Yu, Changlin Tian, Jingwen Li, Hsin-Yung Yen, Sin Man Lam, Guanghou Shui, Xiuna Yang, Yuna Sun, Xuemei Li, Minze Jia, Cheng Yang, Biao Jiang, Zhiyong Lou, Carol V. Robinson, Luet-Lok Wong, Luke W. Guddat, Fei Sun, Quan Wang, Zihe Rao |
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发表年度: | 2018-10-31 |
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摘要: | We report a 3.5-? 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. |
英文摘要: | We report a 3.5-? 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. |
刊物名称: | Science |
英文刊物名称: | Science |
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其它备注: | Hongri Gong, Jun Li, Ao Xu, Yanting Tang, Wenxin Ji, Ruogu Gao, Shuhui Wang, Lu Yu, Changlin Tian, Jingwen Li, Hsin-Yung Yen, Sin Man Lam, Guanghou Shui, Xiuna Yang, Yuna Sun, Xuemei Li, Minze Jia, Cheng Yang, Biao Jiang, Zhiyong Lou, Carol V. Robinson, Luet-Lok Wong, Luke W. Guddat, Fei Sun, Quan Wang, Zihe Rao. An Electron Transfer Path Connects Subunits of a Mycobacterial Respiratory Supercomplex. Science. DOI:10.1126/science.aat8923 |
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