A Common Interface on Histidine-containing Phosphocarrier Protein for Interaction with Its Partner Proteins

• Published in: The Journal of biological chemistry 2000-06, Vol.275 (22), p.16401-16403
• Main Authors: Wang, Guangshun, Sondej, Melissa, Garrett, Daniel S., Peterkofsky, Alan, Clore, G.Marius
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Escherichia coli - metabolism; Magnetic Resonance Spectroscopy; Models, Molecular; Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry; Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism; Protein Binding
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.C000167200

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.