Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis.

Autor: Tan YZ; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, 10032, USA.; National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027, USA., Rodrigues J; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157, Oeiras, Portugal., Keener JE; Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, 85721, USA., Zheng RB; Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada., Brunton R; Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada., Kloss B; Center on Membrane Protein Production and Analysis, New York Structural Biology Center, New York, NY, 10027, USA., Giacometti SI; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, 10032, USA., Rosário AL; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157, Oeiras, Portugal., Zhang L; Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, 35294, USA., Niederweis M; Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, 35294, USA., Clarke OB; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, 10032, USA.; Department of Anesthesiology, Columbia University, New York, NY, 10032, USA., Lowary TL; Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada.; Institute of Biological Chemistry, Academia Sinica, Academia Road, Section 2, #128, Nangang, Taipei, 11529, Taiwan., Marty MT; Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, 85721, USA.; Bio5 Institute, University of Arizona, Tucson, AZ, 85721, USA., Archer M; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157, Oeiras, Portugal., Potter CS; National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027, USA.; Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027, USA.; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, 10032, USA., Carragher B; National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027, USA. bcarr@nysbc.org.; Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027, USA. bcarr@nysbc.org.; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, 10032, USA. bcarr@nysbc.org., Mancia F; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, 10032, USA. fm123@cumc.columbia.edu.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2020 Jul 07; Vol. 11 (1), pp. 3396. Date of Electronic Publication: 2020 Jul 07.
DOI: 10.1038/s41467-020-17202-8
Abstrakt: 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.
Databáze: MEDLINE