Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41467-020-17202-8
Title: Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
Authors: Tan, Yong Zi 
Rodrigues, Jose
Keener, James E
Zheng, Ruixiang Blake
Brunton, Richard
Kloss, Brian
Giacometti, Sabrina
Rosario, Ana L
Zhang, Lei
Niederweis, Michael
Clarke, Oliver B
Lowary, Todd L
Marty, Michael T
Archer, Margarida
Potter, Clinton S
Carragher, Bridget
Mancia, Filippo
Keywords: Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
ETHAMBUTOL RESISTANCE
MOLECULAR-BASIS
TUBERCULOSIS
SINGLE
BIOSYNTHESIS
DISEASE
COMPLEX
MODEL
GENE
ARABINOFURANOSYLTRANSFERASE
Issue Date: 7-Jul-2020
Publisher: NATURE PUBLISHING GROUP
Citation: Tan, Yong Zi, Rodrigues, Jose, Keener, James E, Zheng, Ruixiang Blake, Brunton, Richard, Kloss, Brian, Giacometti, Sabrina, Rosario, Ana L, Zhang, Lei, Niederweis, Michael, Clarke, Oliver B, Lowary, Todd L, Marty, Michael T, Archer, Margarida, Potter, Clinton S, Carragher, Bridget, Mancia, Filippo (2020-07-07). Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. NATURE COMMUNICATIONS 11 (1). ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-020-17202-8
Abstract: Arabinosyltransferase B (EmbB) belongs to a family of membrane-bound glycosyltransferases that build the lipidated polysaccharides of the mycobacterial cell envelope, and are targets of anti-tuberculosis drug ethambutol. We present the 3.3 Å resolution single-particle cryo-electron microscopy structure of Mycobacterium smegmatis EmbB, providing insights on substrate binding and reaction mechanism. Mutations that confer ethambutol resistance map mostly around the putative active site, suggesting this to be the location of drug binding.
Source Title: NATURE COMMUNICATIONS
URI: https://scholarbank.nus.edu.sg/handle/10635/227201
ISSN: 20411723
DOI: 10.1038/s41467-020-17202-8
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