Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

The cryo-EM structure of Mycobacterium smegmatis arabinosyltransferase B EmbB involved in mycobacterial cell wall biosynthesis provides insights into the substrate binding and reaction mechanism. Mapping of the ethambutol resistance associated mutations onto the structure suggests the location of th...

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Autores principales:	Yong Zi Tan, José Rodrigues, James E. Keener, Ruixiang Blake Zheng, Richard Brunton, Brian Kloss, Sabrina I. Giacometti, Ana L. Rosário, Lei Zhang, Michael Niederweis, Oliver B. Clarke, Todd L. Lowary, Michael T. Marty, Margarida Archer, Clinton S. Potter, Bridget Carragher, Filippo Mancia
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/eeb46691fab54cb4aea7d475e6b51125
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spelling	oai:doaj.org-article:eeb46691fab54cb4aea7d475e6b511252021-12-02T16:14:58ZCryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis10.1038/s41467-020-17202-82041-1723https://doaj.org/article/eeb46691fab54cb4aea7d475e6b511252020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17202-8https://doaj.org/toc/2041-1723The cryo-EM structure of Mycobacterium smegmatis arabinosyltransferase B EmbB involved in mycobacterial cell wall biosynthesis provides insights into the substrate binding and reaction mechanism. Mapping of the ethambutol resistance associated mutations onto the structure suggests the location of the drug binding site.Yong Zi TanJosé RodriguesJames E. KeenerRuixiang Blake ZhengRichard BruntonBrian KlossSabrina I. GiacomettiAna L. RosárioLei ZhangMichael NiederweisOliver B. ClarkeTodd L. LowaryMichael T. MartyMargarida ArcherClinton S. PotterBridget CarragherFilippo ManciaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yong Zi Tan José Rodrigues James E. Keener Ruixiang Blake Zheng Richard Brunton Brian Kloss Sabrina I. Giacometti Ana L. Rosário Lei Zhang Michael Niederweis Oliver B. Clarke Todd L. Lowary Michael T. Marty Margarida Archer Clinton S. Potter Bridget Carragher Filippo Mancia Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
description	The cryo-EM structure of Mycobacterium smegmatis arabinosyltransferase B EmbB involved in mycobacterial cell wall biosynthesis provides insights into the substrate binding and reaction mechanism. Mapping of the ethambutol resistance associated mutations onto the structure suggests the location of the drug binding site.
format	article
author	Yong Zi Tan José Rodrigues James E. Keener Ruixiang Blake Zheng Richard Brunton Brian Kloss Sabrina I. Giacometti Ana L. Rosário Lei Zhang Michael Niederweis Oliver B. Clarke Todd L. Lowary Michael T. Marty Margarida Archer Clinton S. Potter Bridget Carragher Filippo Mancia
author_facet	Yong Zi Tan José Rodrigues James E. Keener Ruixiang Blake Zheng Richard Brunton Brian Kloss Sabrina I. Giacometti Ana L. Rosário Lei Zhang Michael Niederweis Oliver B. Clarke Todd L. Lowary Michael T. Marty Margarida Archer Clinton S. Potter Bridget Carragher Filippo Mancia
author_sort	Yong Zi Tan
title	Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
title_short	Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
title_full	Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
title_fullStr	Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
title_full_unstemmed	Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
title_sort	cryo-em structure of arabinosyltransferase embb from mycobacterium smegmatis
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/eeb46691fab54cb4aea7d475e6b51125
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Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

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