Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution.
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.
Kang
C H
CH
Graduate Division of Biophysics, University of California, Berkeley 94720.
Shin
W C
WC
Yamagata
Y
Y
Gokcen
S
S
Ames
G F
GF
Kim
S H
SH
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
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins