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-Structure paper
タイトル | Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 4245, Year 2020 |
掲載日 | 2020年8月25日 |
著者 | 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 要旨 | 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. |
リンク | Nat Commun / PubMed:32843629 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.84 Å |
構造データ | |
化合物 | ChemComp-PEV: ChemComp-HEM: ChemComp-MQ9: ChemComp-CDL: ChemComp-LPP: ChemComp-PIE: ChemComp-FAD: ChemComp-FES: ChemComp-SF4: ChemComp-F3S: |
由来 |
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キーワード | OXIDOREDUCTASE / electron transfer chain / trimer |