An electron transfer path connects subunits of a mycobacterial respiratory supercomplex | Zendy

Hongri Gong | Zendy; Jun Li | Zendy; Ao Xu | Zendy; Yanting Tang | Zendy; Wenxin Ji | Zendy; Ruogu Gao | Zendy; Shuhui Wang | Zendy; Lu Yu | Zendy; Changlin Tian | Zendy; Jingwen Li | Zendy; HsinYung Yen | Zendy; Sin Man Lam | Zendy; Guanghou Shui | Zendy; Xiuna Yang | Zendy; Yuna Sun | Zendy; Xuemei Li | Zendy; Minze Jia | Zendy; Cheng Yang | Zendy; Biao Jiang | Zendy; Zhiyong Lou | Zendy; Carol V. Robinson | Zendy; LuetLok Wong | Zendy; Luke W. Guddat | Zendy; Fei Sun | Zendy; Quan Wang | Zendy; Zihe Rao | Zendy

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An electron transfer path connects subunits of a mycobacterial respiratory supercomplex

Author(s) -

Hongri Gong,

Jun Li,

Ao Xu,

Yanting Tang,

Wenxin Ji,

Ruogu Gao,

Shuhui Wang,

Lu Yu,

Changlin Tian,

Jingwen Li,

HsinYung Yen,

Sin Man Lam,

Guanghou Shui,

Xiuna Yang,

Yuna Sun,

Xuemei Li,

Minze Jia,

Cheng Yang,

Biao Jiang,

Zhiyong Lou,

Carol V. Robinson,

LuetLok Wong,

Luke W. Guddat,

Fei Sun,

Quan Wang,

Zihe Rao

Publication year - 2018

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aat8923

Subject(s) - periplasmic space , protein subunit , mycobacterium smegmatis , coenzyme q – cytochrome c reductase , chemistry , electron transport chain , electron transfer , biophysics , biochemistry , cytochrome c , biology , mitochondrion , mycobacterium tuberculosis , photochemistry , escherichia coli , medicine , tuberculosis , pathology , gene

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.

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