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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Bibliographic Details
Main Authors: 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
Format: article
Language:EN
Published: Nature Portfolio 2020
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Online Access:https://doaj.org/article/eeb46691fab54cb4aea7d475e6b51125
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Summary: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.