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-Structure paper
Title | An electron transfer path connects subunits of a mycobacterial respiratory supercomplex. |
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Journal, issue, pages | Science, Vol. 362, Issue 6418, Year 2018 |
Publish date | Nov 30, 2018 |
![]() | 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 / ![]() ![]() ![]() |
PubMed Abstract | 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 ...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. |
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Methods | EM (single particle) |
Resolution | 3.5 Å |
Structure data | |
Chemicals | ![]() ChemComp-CU: ![]() ChemComp-HEA: ![]() ChemComp-CDL: ![]() ChemComp-9Y0: ![]() ChemComp-PLM: ![]() ChemComp-9XX: ![]() ChemComp-9YF: ![]() ChemComp-HEM: ![]() ChemComp-MQ9: ![]() ChemComp-HEC: ![]() ChemComp-FES: |
Source |
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![]() | ELECTRON TRANSPORT / Respiratory / Supercomplex / SOD / Mycobacterium / ETC / Lipoprotein |