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The role of trimerization in the osmoregulated betaine transporter BetP

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

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Khafizov,  Kamil
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;

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Citation

Perez, C., Khafizov, K., Forrest, L. R., Krämer, R., & Ziegler, C. (2011). The role of trimerization in the osmoregulated betaine transporter BetP. EMBO Reports, 12(8), 804-810.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D639-2
Abstract
The osmoregulated betaine transporter BetP is a stable trimer. Structural studies have shown that individual protomers can adopt distinct transport conformations, implying a functional role for the trimeric state in transport, although the role of trimerization in regulation is not yet understood. We designed putative monomeric mutants by molecular-dynamics simulations and in silico alanine-scanning mutagenesis. Several mutants including BetP-W101A/T351A were monomeric in detergent as well as in the membrane, as shown by blue native gel electrophoresis, crosslinking and electron microscopy. This monomeric form retains the ability to accumulate betaine, but is no longer regulated by hyperosmotic shock.