Regulative interactions of the osmosensing C-terminal domain in the trimeric 
glycine betaine transporter BetP from Corynebacterium glutamicum

Krämer, Reinhard; Ziegler, Christine

doi:10.1515/BC.2009.068

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacterium glutamicum

MPS-Authors

/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

Krämer, R., & Ziegler, C. (2009). Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacterium glutamicum. Biological Chemistry, 390(8), 685-691. doi:10.1515/BC.2009.068.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D7D9-0

Abstract

Activation of the osmoregulated trimeric betaine transporter BetP from Corynebacterium glutamicum was shown to depend mainly on the correct folding and integrity of its 55 amino acid long, partly alpha-helical C-terminal domain. Reorientation of the three C-terminal domains in the BetP trimer indicates different lipid-protein and protein-protein interactions of the C-terminal domain during osmoregulation. A regulation mechanism is suggested where this domain switches the transporter from the inactive to the active state. Interpretation of recently obtained electron and X-ray crystallography data of BetP led to a structure-function based model of C-terminal molecular switching involved in osmoregulation.