X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity.
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-A resolution. In addition, two closed ligand-bound structures of the same protein are presented, a phenylalanine-bound form at 1.8 A and a leucine-bound structure at a nominal resolution of 2.4 A. 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.
Magnusson
Ulrika
U
Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, S-751 24 Uppsala, Sweden.
Salopek-Sondi
Branka
B
Luck
Linda A
LA
Mowbray
Sherry L
SL
D001665:Binding Sites; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D008024:Ligands; D033902:Periplasmic Binding Proteins / Q000737:chemistry*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; D008024:Ligands; C024913:LivK protein, E coli; D033902:Periplasmic Binding Proteins