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Research article - Peer-reviewed, 2004

X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity

Magnusson U, Salopek-Sondi B, Luck LA, Mowbray SL

Abstract

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-Angstrom resolution. In addition, two closed ligand-bound structures of the same protein are presented, a phenylalanine-bound form at 1.8 Angstrom and a leucine-bound structure at a nominal resolution of 2.4 Angstrom. 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

Published in

Journal of Biological Chemistry
2004, Volume: 279, number: 10, pages: 8747-8752
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

      SLU Authors

    • Mowbray, Sherry

      • Department of Molecular Biology, Swedish University of Agricultural Sciences

    Publication identifier

    DOI: https://doi.org/10.1074/jbc.M311890200

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/4821