Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
AuthorTan, Yong Zi
Keener, James E
Zheng, Ruixiang Blake
Giacometti, Sabrina I
Rosário, Ana L
Clarke, Oliver B
Lowary, Todd L
Marty, Michael T
Potter, Clinton S
AffiliationUniv Arizona, Dept Chem & Biochem
Univ Arizona, Bio5 Inst
MetadataShow full item record
PublisherNATURE PUBLISHING GROUP
CitationTan, Y. Z., Rodrigues, J., Keener, J. E., Zheng, R. B., Brunton, R., Kloss, B., ... & Mancia, F. (2020). Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. Nature communications, 11(1), 1-10.
Rights© The Author(s) 2020. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License.
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AbstractArabinosyltransferase B (EmbB) belongs to a family of membrane-bound glycosyl-transferases that build the lipidated polysaccharides of the mycobacterial cell envelope, and are targets of anti-tuberculosis drug ethambutol. We present the 3.3 angstrom 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.
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Except where otherwise noted, this item's license is described as © The Author(s) 2020. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License.
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