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

A. Peterkofsky, G. Wang, D. S. Garrett, B. R. Lee, Y. J. Seaok, G. M. Clore

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


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 IIAGlc have been elucidated. An analysis of the binding interfaces of HPr with enzyme I, IIAGlc and glycogen phosphorylase revealed that a common surface on HPr is involved in all these interactions. Similarly, a common surface on IIAGlc interacts with HPr, IIBGlc and glycerol kinase. Thus, there is a common motif for the protein-protein interactions characteristic of the PTS.

Original languageEnglish (US)
Pages (from-to)347-354
Number of pages8
JournalJournal of Molecular Microbiology and Biotechnology
Issue number3
StatePublished - 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology
  • Applied Microbiology and Biotechnology
  • Molecular Biology


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