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

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.

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 Creators:
Perez, Camilo1, Author           
Faust, Belinda1, Author           
Mehdipour, Ahmad Reza2, Author           
Francesconi, Kevin A.3, Author
Forrest, Lucy R.2, Author           
Ziegler, Christine1, 4, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Max Planck Research Group of Computational Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_persistent22              
3Institute of Chemistry—Analytical Chemistry, University of Graz, Graz 8010, Austria, ou_persistent22              
4Institute of Biophysics and Biophysical Chemistry, University of Regensburg, Regensburg 95053, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 20142014-05-282014-07-15
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/ncomms5231
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: 11 Volume / Issue: 5 Sequence Number: 4231 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723