1usi
From Proteopedia
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L-LEUCINE-BINDING PROTEIN WITH PHENYLALANINE BOUND
Overview
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.
About this Structure
1USI is a [Single protein] structure of sequence from [Escherichia coli] with PHE as [ligand]. Full crystallographic information is available from [OCA].
Reference
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, J Biol Chem. 2004 Mar 5;279(10):8747-52. Epub 2003 Dec 12. PMID:14672931
Page seeded by OCA on Mon Oct 29 21:16:16 2007
