19F NMR evidence for interactions between the c-AMP binding sites on the c-AMP receptor protein from E. coli.
The 19F NMR spectra of 3-fluorotyrosine containing c-AMP receptor protein (CRP) from E. coli have been recorded in the presence of increasing amounts of c-AMP. One of the signals (from Tyr B) shifts upfield by 0.6 ppm in the presence of excess c-AMP and shows both slow and fast exchange behaviour during the titration. This is evidence for interactions between the two c-AMP binding sites on the CRP dimer leading to different dissociation rate constants (less than or equal to 75 s-1; greater than or equal to 350 s-1) for complexes containing one and two c-AMP molecules.
Hinds
M G
MG
Laboratory of Molecular Structure, National Institute for Medical Research, London, UK.
King
R W
RW
Feeney
J
J
D001665:Binding Sites; D000242:Cyclic AMP / Q000378:metabolism*; D002373:Cyclic AMP Receptor Protein / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D005461:Fluorine; D009682:Magnetic Resonance Spectroscopy
D002373:Cyclic AMP Receptor Protein; D005461:Fluorine; D000242:Cyclic AMP