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.
Original language | English (US) |
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Article number | 3396 |
Journal | Nature communications |
Volume | 11 |
Issue number | 1 |
DOIs | |
State | Published - Dec 1 2020 |
ASJC Scopus subject areas
- General Chemistry
- General Biochemistry, Genetics and Molecular Biology
- General Physics and Astronomy
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Single-Particle Cryo-EM Structure of Arabinosyltransferase EmbB from Mycobacterium smegmatis
Tan, Y. Z. (Contributor), Rodrigues, J. (Contributor), Keener, J. E. (Contributor), Zheng, R. B. (Contributor), Brunton, R. (Contributor), Kloss, B. (Contributor), Giacometti, S. I. (Contributor), Rosário, A. L. (Contributor), Zhang, L. (Contributor), Niederweis, M. (Contributor), Clarke, O. B. (Contributor), Lowary, T. L. (Contributor), Marty, M. T. (Contributor), Archer, M. (Contributor), Potter, C. S. (Contributor), Carragher, B. (Contributor) & Mancia, F. (Contributor), Protein Data Bank (PDB), Jun 10 2020
DOI: 10.2210/pdb6X0O/pdb, https://www.wwpdb.org/pdb?id=pdb_00006x0o
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