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

J Mol Microbiol Biotechnol. 2001 Jul;3(3):347-54.


The bacterial phosphoenolpyruvate: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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Binding Sites
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphoenolpyruvate / metabolism
  • Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
  • Protein Conformation
  • Protein Structure, Secondary


  • Bacterial Proteins
  • Escherichia coli Proteins
  • crr protein, E coli
  • Phosphoenolpyruvate
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphocarrier protein HPr