Three-dimensional structures of protein-protein complexes in the E. coli PTS

The bacterial phoaphoenolpyruvate:sugar phosphotransferase system (PTS) includes a collection of proteins that accomplish phosphoryl transfer from phosphoenolpyruvate (PEP) to a sugar in the course of transport. The soluble proteins of the glucose transport pathway also function as regulators of diverse systems. The mechanism of interaction of the phosphoryl carrier proteins with each other as well as with their regulation targets has been amenable to study by nuclear magnetic resonance (NMR) spectroscopy. The three-dimensional solution structures of the complexes between the N-terminal domain of enzyme I and HPr and between HPr and enzyme IIA^Glc have been elucidated. An analysis of the binding interfaces of HPr with enzyme I, IIA^Glc and glycogen phosphorylase revealed that a common surface on HPr is involved in all these interactions. Similarly, a common surface on IIA^Glc interacts with HPr, IIB^Glc and glycerol kinase. Thus, there is a common motif for the protein-protein interactions characteristic of the PTS.