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  Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline

Preiss, L., Langer, J. D., Yildiz, Ö., Eckhardt-Strelau, L., Guillemont, J. E. G., Koul, A., et al. (2015). Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline. Science Advances, 1(4), 1-8. doi:10.1126/sciadv.1500106.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-F00D-D Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-1CF9-E
Genre: Journal Article

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 Creators:
Preiss, Laura1, Author           
Langer, Julian D.2, Author           
Yildiz, Özkan1, Author           
Eckhardt-Strelau, Luise1, Author           
Guillemont, Jérôme E. G.3, Author
Koul, Anil4, Author
Meier, Thomas1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Johnson & Johnson Pharmaceutical Research and Development, Campus de Maigremont-BP615, 27106 Val de Reuil Cedex, France, ou_persistent22              
4Department of Respiratory Infections, Infectious Diseases and Vaccines Group, Janssen Research and Development, Johnson & Johnson, Turnhoutseweg 30, B-2340 Beerse, Belgium, ou_persistent22              

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Free keywords: Tuberculosis (TB) antibiotics; F1Fo-ATP synthase rotor; c-ring; X-ray crystallography; membrane protein structure; Bedaquiline (BDQ); SirturoTM; drug binding; inhibition mechanism
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Language(s): eng - English
 Dates: 20152015
 Publication Status: Published online
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/sciadv.1500106
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Title: Science Advances
Source Genre: Journal
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Pages: - Volume / Issue: 1 (4) Sequence Number: - Start / End Page: 1 - 8 Identifier: -