Abstract
Histidine-containing protein (HPr) is a central component of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS). This brief review covers recent structure-function studies on the active center of this protein: the role of the active center residues in phosphotransferase; the residues contributing to the phosphohydrolysis properties of HPr; and the contribution residues in HPr make to the pKa of the transiently phosphorylated active-site residue, His 15. As well, the potential for HPr to be used as a model protein for studying problems not directly associated with its function in the PTS is discussed.
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