Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF

doi:10.1038/s41467-020-18011-9

	Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF
	Gong, Hongri 1; Gao, Yan 2; Zhou, Xiaoting 3,4; Xiao, Yu 3,4; Wang, Weiwei 3,4; Tang, Yanting 1; Zhou, Shan 1; Zhang, Yuying 1; Ji, Wenxin 5; Yu, Lu 6
刊名	NATURE COMMUNICATIONS
	2020-08-25
卷号	11
ISSN号	2041-1723
DOI	10.1038/s41467-020-18011-9
通讯作者	Gong, Hongri(gonghr@nankai.edu.cn) ; Wang, Quan(wangq@ibp.ac.cn) ; Rao, Zihe(raozh@tsinghua.edu.cn)
英文摘要	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 angstrom 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 3kDa 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.
资助项目	National Key Research and Development Program of China[2017YFC0840300] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XDB37030201] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XDB37020203] ; National Natural Science Foundation of China[81520108019] ; National Natural Science Foundation of China[813300237]
WOS关键词	TRANSMEMBRANE PROTON-TRANSFER ; FUMARATE REDUCTASE ; COMPLEX-II ; ELECTRON-TRANSFER ; MENAQUINONE OXIDOREDUCTASE ; WOLINELLA-SUCCINOGENES ; QUINONE REDUCTASE ; ACTIVE-SITE ; OXIDATION ; PHOSPHORYLATION
WOS研究方向	Science & Technology - Other Topics
语种	英语
出版者	NATURE PUBLISHING GROUP
WOS记录号	WOS:000567537300004
资助机构	National Key Research and Development Program of China ; Strategic Priority Research Program of the Chinese Academy of Sciences ; National Natural Science Foundation of China
内容类型	期刊论文
源URL	[http://ir.hfcas.ac.cn:8080/handle/334002/104054]
专题	中国科学院合肥物质科学研究院
通讯作者	Gong, Hongri; Wang, Quan; Rao, Zihe
作者单位	1.Nankai Univ, Coll Life Sci, Frontiers Sci Ctr Cell Responses, State Key Lab Med Chem Biol, Tianjin 300353, Peoples R China 2.Tsinghua Univ, Lab Struct Biol, Beijing 100084, Peoples R China 3.ShanghaiTech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai 201210, Peoples R China 4.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China 5.Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Omol, Beijing 100101, Peoples R China 6.Chinese Acad Sci, High Magnet Field Lab, Hefei 230031, Peoples R China 7.Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230027, Peoples R China 8.Univ Sci & Technol China, Sch Life Sci, Hefei 230027, Peoples R China 9.Chinese Acad Sci, State Key Lab Mol Dev Biol, Inst Genet & Dev Biol, Beijing 100101, Peoples R China 10.Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia
推荐引用方式 GB/T 7714	Gong, Hongri,Gao, Yan,Zhou, Xiaoting,et al. Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF[J]. NATURE COMMUNICATIONS,2020,11.
APA	Gong, Hongri.,Gao, Yan.,Zhou, Xiaoting.,Xiao, Yu.,Wang, Weiwei.,...&Rao, Zihe.(2020).Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF.NATURE COMMUNICATIONS,11.
MLA	Gong, Hongri,et al."Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF".NATURE COMMUNICATIONS 11(2020).