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

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 nati...

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Published in:The Journal of biological chemistry 2004-02, Vol.279 (7), p.5588
Main Authors: André Schiefner, Jason Breed, Linda Bösser, Susanne Kneip, Jutta Gade, Gudrun Holtmann, Kay Diederichs, Wolfram Welte, Erhard Bremer
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container_issue 7
container_start_page 5588
container_title The Journal of biological chemistry
container_volume 279
creator André Schiefner
Jason Breed
Linda Bösser
Susanne Kneip
Jutta Gade
Gudrun Holtmann
Kay Diederichs
Wolfram Welte
Erhard Bremer
description 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-π 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.
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title Cation-π Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli
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