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Cryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism

Authors
  • Saridakis, Emmanuel1, 2
  • Vishwakarma, Rishi3, 4
  • Lai-Kee-Him, Josephine3
  • Martin, Kevin3
  • Simon, Isabelle5, 6
  • Cohen-Gonsaud, Martin3
  • Coste, Franck6
  • Bron, Patrick3
  • Margeat, Emmanuel3
  • Boudvillain, Marc2, 6
  • 1 Institute of Nanoscience and Nanotechnology, NCSR “Demokritos”, Ag. Paraskevi, Athens, 15310, Greece , Athens (Greece)
  • 2 Le Studium Loire Valley Institute for Advanced Studies, Orléans, France , Orléans (France)
  • 3 Univ Montpellier, CNRS, INSERM, Montpellier, France , Montpellier (France)
  • 4 The Pennsylvania State University, University Park, State College, PA, 16802, USA , State College (United States)
  • 5 Université d’Orléans, Orléans, France , Orléans (France)
  • 6 affiliated with Université d’Orléans, Orléans, cedex 2, 45071, France , Orléans (France)
Type
Published Article
Journal
Communications Biology
Publisher
Nature Publishing Group UK
Publication Date
Feb 09, 2022
Volume
5
Issue
1
Identifiers
DOI: 10.1038/s42003-022-03069-6
Source
Springer Nature
Disciplines
  • article
License
Green

Abstract

Cryo-EM shows that M. tuberculosis Rho-factor adopts an open, ring-shaped hexamer conformation and a steric bulk in the cavity for bicyclomycin binding, which explains resistance to the antibiotic.

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