Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
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Univ Arizona, Dept Chem & BiochemUniv Arizona, Bio5 Inst
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2020-07-07Metadata
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NATURE PUBLISHING GROUPCitation
Tan, 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.Journal
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© The Author(s) 2020. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License.Collection Information
This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.Abstract
Arabinosyltransferase 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.Note
Open access journalISSN
2041-1723PubMed ID
32636380Version
Final published versionScopus Count
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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.