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  Inward-facing conformation of a multidrug resistance MATE family transporter

Zakrzewska, S., Mehdipour, A. R., Malviya, V. N., Nonaka, T., Koepke, J., Muenke, C., et al. (2019). Inward-facing conformation of a multidrug resistance MATE family transporter. Proceedings of the National Academy of Sciences of the United States of America, 116(25), 12275-12284. doi:10.1073/pnas.1904210116.

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 Creators:
Zakrzewska, Sandra1, Author              
Mehdipour, Ahmad Reza2, Author              
Malviya, Viveka Nand1, Author              
Nonaka, Tsuyoshi1, Author              
Koepke, Jürgen1, Author              
Muenke, Cornelia1, Author              
Hausner, Winfried3, Author
Hummer, Gerhard2, 4, Author              
Safarian, Schara1, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
3Faculty of Microbiology, University of Regensburg, 93053 Regensburg, Germany, ou_persistent22              
4Institute of Biophysics, Goethe University, 60438 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: multidrug resistance; membrane protein structure; MATE transporter; inward-facing conformation; lipids
 Abstract: Multidrug and toxic compound extrusion (MATE) transporters mediate excretion of xenobiotics and toxic metabolites, thereby conferring multidrug resistance in bacterial pathogens and cancer cells. Structural information on the alternate conformational states and knowledge of the detailed mechanism of MATE transport are of great importance for drug development. However, the structures of MATE transporters are only known in V-shaped outward-facing conformations. Here, we present the crystal structure of a MATE transporter from Pyrococcus furiosus (PfMATE) in the long-sought-after inward-facing state, which was obtained after crystallization in the presence of native lipids. Transition from the outward-facing state to the inward-facing state involves rigid body movements of transmembrane helices (TMs) 2–6 and 8–12 to form an inverted V, facilitated by a loose binding of TM1 and TM7 to their respective bundles and their conformational flexibility. The inward-facing structure of PfMATE in combination with the outward-facing one supports an alternating access mechanism for the MATE family transporters

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Language(s): eng - English
 Dates: 2019-03-12201920192019-06-032019-06-18
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1904210116
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 116 (25) Sequence Number: - Start / End Page: 12275 - 12284 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230