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  Substrate specificity and ion coupling in the Na+/betaine symporter BetP

Perez, C., Koshy, C., Ressl, S., Nicklisch, S., Krämer, R., & Ziegler, C. (2011). Substrate specificity and ion coupling in the Na+/betaine symporter BetP. EMBO Journal, 30, 1221-1229. doi:10.1038/emboj.2011.46.

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 Creators:
Perez, Camilo1, Author           
Koshy, Caroline1, Author           
Ressl, Susanne1, 2, Author           
Nicklisch, Sascha3, 4, Author
Krämer, Reinhard3, Author
Ziegler, Christine1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Departments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Structural Biology, and Photon Science, The Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA, ou_persistent22              
3Institute of Biochemistry, University of Cologne, Köln, Germany, ou_persistent22              
4Marine Science Institute, University of California, Santa Barbara, CA, USA, ou_persistent22              

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Free keywords: alternating access; H+ and Na+ coupling; inverted repeats; membrane transport; substrate specificity
 Abstract: BetP is an Na+-coupled betaine-specific transporter of the betaine–choline–carnitine (BCC) transporter family involved in the response to hyperosmotic stress. The crystal structure of BetP revealed an overall fold of two inverted structurally related repeats (LeuT-fold) that BetP shares with other sequence-unrelated Na+-coupled symporters. Numerous structures of LeuT-fold transporters in distinct conformational states have contributed substantially to our understanding of the alternating access mechanism of transport. Nevertheless, coupling of substrate and co-transported ion fluxes has not been structurally corroborated to the same extent. We converted BetP by a single-point mutation—glycine to aspartate—into an H+-coupled choline-specific transporter and solved the crystal structure of this mutant in complex with choline. The structure of BetP-G153D demonstrates a new inward-facing open conformation for BetP. Choline binding to a location close to the second, low-affinity sodium-binding site (Na2) of LeuT-fold transporters is facilitated by the introduced aspartate. Our data confirm the importance of a cation-binding site in BetP, playing a key role in a proposed molecular mechanism of Na+ and H+ coupling in BCC transporters.

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Language(s): eng - English
 Dates: 2010-10-302011-01-312011-03-012011-04-06
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/emboj.2011.46
PMID: 21364531
PMC: PMC3094121
 Degree: -

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Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 30 Sequence Number: - Start / End Page: 1221 - 1229 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061