Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

Yong Zi Tan, José Rodrigues, James E. Keener, Ruixiang Blake Zheng, Richard Brunton, Brian Kloss, Sabrina I. Giacometti, Ana L. Rosário, Lei Zhang, Michael Niederweis, Oliver B. Clarke, Todd L. Lowary, Michael T. Marty, Margarida Archer, Clinton S. Potter, Bridget Carragher, Filippo Mancia

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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 languageEnglish (US)
Article number3396
JournalNature communications
Issue number1
StatePublished - Dec 1 2020

ASJC Scopus subject areas

  • General Chemistry
  • General Biochemistry, Genetics and Molecular Biology
  • General Physics and Astronomy


Dive into the research topics of 'Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis'. Together they form a unique fingerprint.

Cite this