Mutational analysis of ligand recognition by tcp, the citrate chemoreceptor of Salmonella enterica serovar typhimurium.
The chemoreceptor Tcp mediates taxis to citrate. To identify citrate-binding residues, we substituted cysteine for seven basic or polar residues that are chosen based on the comparison of Tcp with the well-characterized chemoreceptors. The results suggest that Arg-63, Arg-68, Arg-72, Lys-75, and Tyr-150 (and probably other unidentified residues) are involved in the recognition of citrate.
Iwama
T
T
Department of Biotechnology, Division of Utilization of Biological Resources, Faculty of Agriculture, Gifu University, Gifu 501-1193, Japan.
Nakao
K I
KI
Nakazato
H
H
Yamagata
S
S
Homma
M
M
Kawagishi
I
I
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001665:Binding Sites / Q000187:drug effects / Q000235:genetics; D002633:Chemotaxis / Q000187:drug effects; D002951:Citrates / Q000494:pharmacology*; D003432:Cross-Linking Reagents; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D012486:Salmonella typhimurium / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D002951:Citrates; D003432:Cross-Linking Reagents; D004220:Disulfides; D008024:Ligands; D008565:Membrane Proteins; C079113:Tcp receptor