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Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling

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Perez,  Camilo
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Faust,  Belinda
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mehdipour,  Ahmad Reza
Max Planck Research Group of Computational Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Forrest,  Lucy R.
Max Planck Research Group of Computational Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ziegler,  Christine
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics and Biophysical Chemistry, University of Regensburg, Regensburg 95053, Germany;

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Citation

Perez, C., Faust, B., Mehdipour, A. R., Francesconi, K. A., Forrest, L. R., & Ziegler, C. (2014). Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling. Nature Communications, 5: 4231. doi:10.1038/ncomms5231.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0026-B2D0-B
Abstract
The Na+-coupled betaine symporter BetP shares a highly conserved fold with other sequence unrelated secondary transporters, for example, with neurotransmitter symporters. Recently, we obtained atomic structures of BetP in distinct conformational states, which elucidated parts of its alternating-access mechanism. Here, we report a structure of BetP in a new outward-open state in complex with an anomalous scattering substrate, adding a fundamental piece to an unprecedented set of structural snapshots for a secondary transporter. In combination with molecular dynamics simulations these structural data highlight important features of the sequential formation of the substrate and sodium-binding sites, in which coordinating water molecules play a crucial role. We observe a strictly interdependent binding of betaine and sodium ions during the coupling process. All three sites undergo progressive reshaping and dehydration during the alternating-access cycle, with the most optimal coordination of all substrates found in the closed state.