title: Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution.
abstract: A wide variety of sugars, amino acids, peptides, and inorganic ions are transported into bacteria by periplasmic transport systems consisting of substrate-specific receptors (binding proteins) and membrane-bound protein complexes. The crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) at 2.7-A resolution shows that the molecule has a bi-lobal structure and that its topological structure is different from other amino acid-binding proteins but is similar to the sulfate-binding protein and maltose-binding protein. High sequence homology between LAO and the histidine-binding protein (HisJ) and the fact that LAO and HisJ share the same membrane-bound protein complex allow one to define functional regions responsible for the ligand binding and for the interaction with the membrane complex.
authors.affiliation: Graduate Division of Biophysics, University of California, Berkeley 94720.
authors.forename: C H
authors.initials: CH
authors.lastname: Kang
authors.forename: W C
authors.initials: WC
authors.lastname: Shin
authors.forename: Y
authors.initials: Y
authors.lastname: Yamagata
authors.forename: S
authors.initials: S
authors.lastname: Gokcen
authors.forename: G F
authors.initials: GF
authors.lastname: Ames
authors.forename: S H
authors.initials: SH
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003198:Computer Simulation; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D012984:Software; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D001426:Bacterial Proteins; D026901:Membrane Transport Proteins