The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB

M. tuberculosis cytochrome bd oxidase is of interest as a TB drug target. Here, the authors present the 2.5 Å cryo-EM structure of M. tuberculosis cytochrome bd oxidase and identify a disulfide bond within the canonical quinol binding and oxidation domain (Q-loop) and a menaquinone-9 binding site at...

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Autores principales:	Schara Safarian, Helen K. Opel-Reading, Di Wu, Ahmad R. Mehdipour, Kiel Hards, Liam K. Harold, Melanie Radloff, Ian Stewart, Sonja Welsch, Gerhard Hummer, Gregory M. Cook, Kurt L. Krause, Hartmut Michel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d59d3dd24560451195a1764a95c9ea6d
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spelling	oai:doaj.org-article:d59d3dd24560451195a1764a95c9ea6d2021-12-02T15:26:52ZThe cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB10.1038/s41467-021-25537-z2041-1723https://doaj.org/article/d59d3dd24560451195a1764a95c9ea6d2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25537-zhttps://doaj.org/toc/2041-1723M. tuberculosis cytochrome bd oxidase is of interest as a TB drug target. Here, the authors present the 2.5 Å cryo-EM structure of M. tuberculosis cytochrome bd oxidase and identify a disulfide bond within the canonical quinol binding and oxidation domain (Q-loop) and a menaquinone-9 binding site at heme b 595.Schara SafarianHelen K. Opel-ReadingDi WuAhmad R. MehdipourKiel HardsLiam K. HaroldMelanie RadloffIan StewartSonja WelschGerhard HummerGregory M. CookKurt L. KrauseHartmut MichelNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Schara Safarian Helen K. Opel-Reading Di Wu Ahmad R. Mehdipour Kiel Hards Liam K. Harold Melanie Radloff Ian Stewart Sonja Welsch Gerhard Hummer Gregory M. Cook Kurt L. Krause Hartmut Michel The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB
description	M. tuberculosis cytochrome bd oxidase is of interest as a TB drug target. Here, the authors present the 2.5 Å cryo-EM structure of M. tuberculosis cytochrome bd oxidase and identify a disulfide bond within the canonical quinol binding and oxidation domain (Q-loop) and a menaquinone-9 binding site at heme b 595.
format	article
author	Schara Safarian Helen K. Opel-Reading Di Wu Ahmad R. Mehdipour Kiel Hards Liam K. Harold Melanie Radloff Ian Stewart Sonja Welsch Gerhard Hummer Gregory M. Cook Kurt L. Krause Hartmut Michel
author_facet	Schara Safarian Helen K. Opel-Reading Di Wu Ahmad R. Mehdipour Kiel Hards Liam K. Harold Melanie Radloff Ian Stewart Sonja Welsch Gerhard Hummer Gregory M. Cook Kurt L. Krause Hartmut Michel
author_sort	Schara Safarian
title	The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB
title_short	The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB
title_full	The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB
title_fullStr	The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB
title_full_unstemmed	The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB
title_sort	cryo-em structure of the bd oxidase from m. tuberculosis reveals a unique structural framework and enables rational drug design to combat tb
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/d59d3dd24560451195a1764a95c9ea6d
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The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB

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