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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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

Reinhard Krämer1 / Christine Ziegler2

1Institute of Biochemistry, University of Cologne, D-50674 Cologne, Germany

2Department of Structural Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 8, Pages 685–691, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.068, May 2009

Publication History

Received:
2009-01-12
Accepted:
2009-03-28
Published Online:
2009-05-09

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 α-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.

Keywords: anionic lipids; glycine betaine; lipid-protein interaction; molecular switch; osmotic stress regulation; structure; transport; trimer

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