+Search query
-Structure paper
Title | Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 4245, Year 2020 |
Publish date | Aug 25, 2020 |
![]() | Hongri Gong / Yan Gao / Xiaoting Zhou / Yu Xiao / Weiwei Wang / Yanting Tang / Shan Zhou / Yuying Zhang / Wenxin Ji / Lu Yu / Changlin Tian / Sin Man Lam / Guanghou Shui / Luke W Guddat / Luet-Lok Wong / Quan Wang / Zihe Rao / ![]() ![]() ![]() |
PubMed Abstract | Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are widespread in Gram-positive bacteria but little is known about the catalytic mechanisms they employ for succinate oxidation by ...Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are widespread in Gram-positive bacteria but little is known about the catalytic mechanisms they employ for succinate oxidation by menaquinone. Here, we present the 2.8 Å cryo-electron microscopy structure of a Mycobacterium smegmatis Sdh, which forms a trimer. We identified the membrane-anchored SdhF as a subunit of the complex. The 3 kDa SdhF forms a single transmembrane helix and this helix plays a role in blocking the canonically proximal quinone-binding site. We also identified two distal quinone-binding sites with bound quinones. One distal binding site is formed by neighboring subunits of the complex. Our structure further reveals the electron/proton transfer pathway for succinate oxidation by menaquinone. Moreover, this study provides further structural insights into the physiological significance of a trimeric respiratory complex II. The structure of the menaquinone binding site could provide a framework for the development of Sdh-selective anti-mycobacterial drugs. |
![]() | ![]() ![]() ![]() |
Methods | EM (single particle) |
Resolution | 2.84 Å |
Structure data | |
Chemicals | ![]() ChemComp-PEV: ![]() ChemComp-HEM: ![]() ChemComp-MQ9: ![]() ChemComp-CDL: ![]() ChemComp-LPP: ![]() ChemComp-PIE: ![]() ChemComp-FAD: ![]() ChemComp-FES: ![]() ChemComp-SF4: ![]() ChemComp-F3S: |
Source |
|
![]() | OXIDOREDUCTASE / electron transfer chain / trimer |