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J. Biol. Chem., Vol. 279, Issue 10, 8747-8752, March 5, 2004

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X-ray Structures of the Leucine-binding Protein Illustrate Conformational Changes and the Basis of Ligand Specificity^*

Ulrika Magnusson, Branka Salopek-Sondi¶, Linda A. Luck, and Sherry L. Mowbray||**

From the Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, S-751 24 Uppsala, Sweden, the Department of Chemistry, Clarkson University, Potsdam, New York 13699, and the ^||Department of Molecular Biosciences, Division of Structural Biology, Swedish University of Agricultural Sciences, Biomedical Center, Box 590, S-751 24 Uppsala, Sweden

The periplasmic leucine-binding protein is the primary receptor for the leucine transport system in Escherichia coli. We report here the structure of an open ligand-free form solved by molecular replacement and refined at 1.5-Å resolution. In addition, two closed ligand-bound structures of the same protein are presented, a phenylalanine-bound form at 1.8 Å and a leucine-bound structure at a nominal resolution of 2.4 Å. These structures show the basis of this protein's ligand specificity, as well as illustrating the conformational changes that are associated with ligand binding. Comparison with earlier structures provides further information about solution conformations, as well as the different specificity of the closely related leucine/isoleucine/valine-binding protein.

Received for publication, October 29, 2003 , and in revised form, December 10, 2003.

^* This work was supported by grants from the Swedish Research Foundation (VR) (to S. L. M.), the Petroleum Research Fund (36825-AC4), National Institutes of Health (RO3-CA 89705) (to L. A. L.) as well as by Uppsala University and the Swedish University of Agricultural Sciences. 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.

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

^¶ Present address: Dept. of Molecular Biology, Rudjer Bokovic Institute, Bijenicka cesta 54, Zagreb, 10 000, Croatia.

^** To whom correspondence should be addressed. Tel.: 46-18-471-49-90; Fax: 46-18-53-69-71; E-mail: mowbray{at}xray.bmc.uu.se.

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