A common interface on histidine-containing phosphocarrier protein for interaction with its partner proteins

Guangshun Wang, Melissa Sondej, Daniel S. Garrett, Alan Peterkofsky, G. Marius Clore

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

The bacterial phosphoenolpyruvate:sugar phosphotransferase system accomplishes both the transport and phosphorylation of sugars as well as the regulation of some cellular processes. An important component of this system is the histidine-containing phosphocarrier protein, HPr, which accepts a phosphoryl group from enzyme I, transfers a phosphoryl group to IIA proteins, and is an allosteric regulator of glycogen phosphorylase. Because the nature of the surface on HPr that interacts with this multiplicity of proteins from Escherichia coli was previously undefined, we investigated these interactions by nuclear magnetic resonance spectroscopy. The chemical shift changes of the backbone and side-chain amide 1H and 15N nuclei of uniformly 15N-labeled HPr in the absence and presence of natural abundance glycogen phosphorylase, glucose-specific enzyme IIA, or the N-terminal domain of enzyme I have been determined. Mapping these chemical shift perturbations onto the three- dimensional structure of HPr permitted us to identify the binding surface(s) of HPr for interaction with these proteins. Here we show that the mapped interfaces on HPr are remarkably similar, indicating that HPr employs a similar surface in binding to its partners.

Original languageEnglish (US)
Pages (from-to)16401-16403
Number of pages3
JournalJournal of Biological Chemistry
Volume275
Issue number22
DOIs
StatePublished - Jun 2 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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