Thirty-four of the 85 residues of the histidine-containing protein HPr of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system have been changed by site-directed mutagenesis. Many of the mutations have wild-type activity suggesting an unaltered tertiary structure but have altered binding to three monoclonal antibodies: Jel42, Jel44, and Jel323. This altered binding defines the residues that are involved in the epitopes of HPr. At present, two different three-dimensional structures have been determined for HPr, one from two-dimensional nuclear magnetic resonance spectra and the other from x-ray diffraction of HPr crystals. The epitope mapping for Jel42 does not distinguish between the tertiary structures. However, only the HPr structure derived from two-dimensional nuclear magnetic resonance spectra is consistent with a contiguous surface binding site that can be defined as the epitope for Jel44. Thus the x-ray structure may represent a partially unfolded HPr.
CITATION STYLE
Sharma, S., Georges, F., Delbaere, L. T. J., Lee, J. S., Klevit, R. E., & Waygood, E. B. (1991). Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-containing protein HPr. Proceedings of the National Academy of Sciences of the United States of America, 88(11), 4877–4881. https://doi.org/10.1073/pnas.88.11.4877
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