1usi

L-leucine-binding protein with phenylalanine bound

spinqualitylabelsall models 1usi, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1usi is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: PHE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LIVK_ECOLI This protein is a component of the leucine-specific transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids in E.coli. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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