English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  DetailsSummary

Released
Journal Article

The role of trimerization in the osmoregulated betaine transporter BetP

MPS-Authors
/persons/resource/persons137833

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

/persons/resource/persons137739

Khafizov,  Kamil
Max Planck Research Group of Computational Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137656

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

/persons/resource/persons137962

Ziegler,  Christine
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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: https://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.