Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels

Cytochromes bd oxidase (Cyt-bd) catalyzes the reduction of oxygen to water and is the terminal oxidase in the respiratory chain of prokaryotes. Here, the authors present the 2.8 Å cryo-EM structure of Mycobacterium smegmatis Cyt-bd and identify two potential oxygen access channels in the structure,...

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Autores principales:	Weiwei Wang, Yan Gao, Yanting Tang, Xiaoting Zhou, Yuezheng Lai, Shan Zhou, Yuying Zhang, Xiuna Yang, Fengjiang Liu, Luke W. Guddat, Quan Wang, Zihe Rao, Hongri Gong
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/96511536ccce4130ad8b504a038a74d9
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spelling	oai:doaj.org-article:96511536ccce4130ad8b504a038a74d92021-12-02T16:13:56ZCryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels10.1038/s41467-021-24924-w2041-1723https://doaj.org/article/96511536ccce4130ad8b504a038a74d92021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24924-whttps://doaj.org/toc/2041-1723Cytochromes bd oxidase (Cyt-bd) catalyzes the reduction of oxygen to water and is the terminal oxidase in the respiratory chain of prokaryotes. Here, the authors present the 2.8 Å cryo-EM structure of Mycobacterium smegmatis Cyt-bd and identify two potential oxygen access channels in the structure, which is of interest for the development of novel antituberculosis drugs.Weiwei WangYan GaoYanting TangXiaoting ZhouYuezheng LaiShan ZhouYuying ZhangXiuna YangFengjiang LiuLuke W. GuddatQuan WangZihe RaoHongri GongNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Weiwei Wang Yan Gao Yanting Tang Xiaoting Zhou Yuezheng Lai Shan Zhou Yuying Zhang Xiuna Yang Fengjiang Liu Luke W. Guddat Quan Wang Zihe Rao Hongri Gong Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
description	Cytochromes bd oxidase (Cyt-bd) catalyzes the reduction of oxygen to water and is the terminal oxidase in the respiratory chain of prokaryotes. Here, the authors present the 2.8 Å cryo-EM structure of Mycobacterium smegmatis Cyt-bd and identify two potential oxygen access channels in the structure, which is of interest for the development of novel antituberculosis drugs.
format	article
author	Weiwei Wang Yan Gao Yanting Tang Xiaoting Zhou Yuezheng Lai Shan Zhou Yuying Zhang Xiuna Yang Fengjiang Liu Luke W. Guddat Quan Wang Zihe Rao Hongri Gong
author_facet	Weiwei Wang Yan Gao Yanting Tang Xiaoting Zhou Yuezheng Lai Shan Zhou Yuying Zhang Xiuna Yang Fengjiang Liu Luke W. Guddat Quan Wang Zihe Rao Hongri Gong
author_sort	Weiwei Wang
title	Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
title_short	Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
title_full	Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
title_fullStr	Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
title_full_unstemmed	Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
title_sort	cryo-em structure of mycobacterial cytochrome bd reveals two oxygen access channels
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/96511536ccce4130ad8b504a038a74d9
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Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels

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