1usg

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{{STRUCTURE_1usg| PDB=1usg | SCENE= }}
{{STRUCTURE_1usg| PDB=1usg | SCENE= }}
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'''L-LEUCINE-BINDING PROTEIN, APO FORM'''
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===L-LEUCINE-BINDING PROTEIN, APO FORM===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_14672931}}
==About this Structure==
==About this Structure==
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[[Category: Transport protein]]
[[Category: Transport protein]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:44:26 2008''

Revision as of 00:44, 29 July 2008

Image:1usg.png

Template:STRUCTURE 1usg

L-LEUCINE-BINDING PROTEIN, APO FORM

Template:ABSTRACT PUBMED 14672931

About this Structure

1USG is a Single protein structure of sequence from Escherichia coli. 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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