Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc.
Enzyme IIAglc and HPr are central regulatory and phosphocarrier proteins of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) of bacteria. During phosphoryl transfer from phosphoenolpyruvate to glucose, phosphate is transferred from HPr to enzyme IIAglc. In order to characterize the binding interfaces of the two proteins during phosphate transfer, 15N-edited and 15N-filtered NMR experiments have been recorded for the complex of enzyme IIAglc and HPr from Bacillus subtilis. Uniformly 15N-labeled enzyme IIAglc and nonlabeled HPr were used in these studies. Residues which undergo significant chemical shift changes upon complex formation have been identified for both proteins. The binding interfaces of the two proteins, suggested by the observed chemical shift changes, involve predominantly hydrophobic surfaces near the active site His-15 of HPr and the phosphoryl acceptor His-83 of IIAglc.
Chen
Y
Y
Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037.
Reizer
J
J
Saier
M H
MH
Fairbrother
W J
WJ
Wright
P E
PE
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004926:Escherichia coli / Q000201:enzymology*; D006639:Histidine; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry / Q000378:metabolism*; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D006639:Histidine; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; C031629:phosphoenolpyruvate-glucose phosphotransferase