1usk
From Proteopedia
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Revision as of 15:05, 5 November 2007
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L-LEUCINE-BINDING PROTEIN WITH LEUCINE 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
1USK is a Single protein structure of sequence from Escherichia coli with LEU as ligand. Structure known Active Site: AC1. 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
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