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 () and Filippo Mancia ()
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Yong Zi Tan: Columbia University
José Rodrigues: Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA)
James E. Keener: University of Arizona
Ruixiang Blake Zheng: University of Alberta
Richard Brunton: University of Alberta
Brian Kloss: Center on Membrane Protein Production and Analysis, New York Structural Biology Center
Sabrina I. Giacometti: Columbia University
Ana L. Rosário: Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA)
Lei Zhang: University of Alabama at Birmingham
Michael Niederweis: University of Alabama at Birmingham
Oliver B. Clarke: Columbia University
Todd L. Lowary: University of Alberta
Michael T. Marty: University of Arizona
Margarida Archer: Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA)
Clinton S. Potter: National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center
Bridget Carragher: National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center
Filippo Mancia: Columbia University

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-17202-8

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