Molecular genetic, biochemical and nuclear magnetic resonance studies on the role of the tryptophan residues of glutamine-binding protein from Escherichia coli.
The results of molecular genetic, biochemical and nuclear magnetic resonance studies on glutamine-binding protein of Escherichia coli suggest that the only two tryptophan residues, at positions 32 and 220, in the protein molecule are likely to be involved in (or sensitive to) interactions with the membrane-bound protein components of the glutamine transport system. It has been found that both tryptophan residues have limited motional freedom, are located away from the surface of the protein molecule and are not close to the ligand-binding site. Their presence, however, is required for the optimal transport of L-glutamine across the cytoplasmic membrane, though not essential for the ligand-binding process. The relevance of these results to the structure and function of the glutamine-binding protein in the glutamine transport system is discussed.
Shen
Q C
QC
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213.
Simplaceanu
V
V
Cottam
P F
PF
Wu
J L
JL
Hong
J S
JS
Ho
C
C
D002352:Carrier Proteins / Q000648:ultrastructure*; D004926:Escherichia coli; D005973:Glutamine / Q000378:metabolism; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D009154:Mutation; D012997:Solvents; D013329:Structure-Activity Relationship; D013696:Temperature; D014364:Tryptophan; D014867:Water
D002352:Carrier Proteins; D008024:Ligands; D012997:Solvents; C037853:glutamine transport proteins; D014867:Water; D005973:Glutamine; D014364:Tryptophan