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J. Biol. Chem., Vol. 279, Issue 7, 5588-5596, February 13, 2004

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Cation- Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli^*

André Schiefner, Jason Breed¶, Linda Bösser||, Susanne Kneip||, Jutta Gade||, Gudrun Holtmann||, Kay Diederichs, Wolfram Welte**, and Erhard Bremer||

From the Fachbereich Biologie, Universität Konstanz, Universitätsstrasse 10, D-78457 Konstanz, Germany and the ^||Fachbereich Biologie, Laboratorium für Mikrobiologie, Philipps-Universität Marburg, Karl-von-Frisch Strasse, D-35032 Marburg, Germany

Compatible solutes such as glycine betaine and proline betaine are accumulated to exceedingly high intracellular levels by many organisms in response to high osmolarity to offset the loss of cell water. They are excluded from the immediate hydration shell of proteins and thereby stabilize their native structure. Despite their exclusion from protein surfaces, the periplasmic ligand-binding protein ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. To understand the mechanism of compatible solute binding, we determined the high resolution structure of ProX in complex with its ligands glycine betaine and proline betaine. This crystallographic study revealed that cation- interactions between the positive charge of the quaternary amine of the ligands and three tryptophan residues forming a rectangular aromatic box are the key determinants of the high affinity binding of compatible solutes by ProX. The structural analysis was combined with site-directed mutagenesis of the ligand binding pocket to estimate the contributions of the tryptophan residues involved in binding.

Received for publication, September 3, 2003 , and in revised form, November 5, 2003.

The atomic coordinates and structure factors (codes 1R9L and 1R9Q) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This study was supported by Deutsche Forschungsgemeinschaft Grant SFB-395, by the Graduiertenkolleg "Proteinfunktion auf atomarer Ebene," by the Max-Planck-Institute for terrestrial Microbiology (Marburg), and by the Fonds der Chemischen Industrie (to E. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^¶ Present address: Astra Zeneca, Mereside, Macclesfield SK10 4TG, UK.

^** To whom correspondence should be addressed. E-mail: wolfram.welte{at}uni-konstanz.de.

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