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Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

Author

Listed:
  • Yong Zi Tan

    (Columbia University
    National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center)

  • 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
    Columbia University)

  • Todd L. Lowary

    (University of Alberta
    Institute of Biological Chemistry, Academia Sinica)

  • Michael T. Marty

    (University of Arizona
    Bio5 Institute, 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
    Simons Electron Microscopy Center, New York Structural Biology Center
    Columbia University)

  • Bridget Carragher

    (National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center
    Simons Electron Microscopy Center, New York Structural Biology Center
    Columbia University)

  • Filippo Mancia

    (Columbia University)

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.

Suggested Citation

  • 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 & Tod, 2020. "Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17202-8
    DOI: 10.1038/s41467-020-17202-8
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