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Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF
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Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF
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Journal Article
Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF
2020
Overview
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.
Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are members of the complex II superfamily. Here, the authors present the 2.8 Å cryo-EM structure of
Mycobacterium smegmatis
Sdh2, which reveals membrane-anchored SdhF as a component of the complex and they discuss the electron/proton transfer pathway in the Sdh2 trimer.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/154
/ 631/326
/ 631/57
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Humanities and Social Sciences
/ Multienzyme Complexes - chemistry
/ Multienzyme Complexes - genetics
/ Multienzyme Complexes - metabolism
/ Mycobacterium smegmatis - chemistry
/ Mycobacterium smegmatis - enzymology
/ Protein Subunits - chemistry
/ Protein Subunits - metabolism
/ Protons
/ Quinones
/ Science
/ Structure-Activity Relationship
/ Succinate Dehydrogenase - chemistry
/ Succinate Dehydrogenase - metabolism
/ Trimers
