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Inward-facing conformation of a multidrug resistance MATE family transporter

MPS-Authors
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Zakrzewska,  Sandra
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mehdipour,  Ahmad Reza
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Malviya,  Viveka Nand
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Nonaka,  Tsuyoshi
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Koepke,  Jürgen
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Muenke,  Cornelia
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hummer,  Gerhard
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics, Goethe University, 60438 Frankfurt am Main, Germany;

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Safarian,  Schara
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-0003-B53C-E
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