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Originally published In Press as doi:10.1074/jbc.C000167200 on April 6, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16401-16403, June 2, 2000
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ACCELERATED PUBLICATION
A Common Interface on Histidine-containing Phosphocarrier Protein for Interaction with Its Partner Proteins*

Guangshun WangDagger , Melissa Sondej§, Daniel S. GarrettDagger , Alan Peterkofsky§, and G. Marius CloreDagger ||

From the Dagger  Laboratory of Chemical Physics, NIDDK, and the § Laboratory of Biochemical Genetics, NHLBI, National Institutes of Health, Bethesda, Maryland 20892

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.

* This work was supported in part by the AIDS Targeted Antiviral Program of the Office of the Director of the National Institutes of Health (to G. M. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence may be addressed: Laboratory of Biochemical Genetics, Bldg. 36, Room 4C-11, NHLBI, National Institutes of Health, Bethesda, MD 20892. E-mail: alan@codon.nih.gov.

|| To whom correspondence may be addressed: Laboratory of Chemical Physics, Bldg. 5, Room BI-30I, NIDDK, National Institutes of Health, Bethesda, MD 20892-0510. E-mail: clore@speck.niddk.nih.gov.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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