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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 |
Appears in Collections: | Staff Publications Elements |
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