Naslov
X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity

Autori
Magnusson, Ulrika ; Salopek-Sondi, Branka ; Luck, Linda A. ; Mowbray, Sherry L.

Izvornik
Journal of Biological Chemistry (0021-9258) 279 (2004), 10; 8747-8752

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Escherichia coli; leucine-binding protein; X-ray structure of ligand-free and ligand-bound form; conformation in solution; ligand specificity

Sažetak
The periplasmatic 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.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA