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J. Biol. Chem., Vol. 281, Issue 43, 32508-32515, October 27, 2006

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Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System^*

JoséA. Márquez¹, Stefan Reinelt¹², Brigitte Koch^¶, Roswitha Engelmann^¶, Wolfgang Hengstenberg^¶, and Klaus Scheffzek³

From the European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstrasse 1, 69117 Heidelberg, Germany, the European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, B. P. 181, 38042 Grenoble Cedex 9, France, and the ^¶AG Physiology of Microorganisms, Ruhr-University-Bochum, D-44780 Bochum, Germany

Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first step of this pathway EI phosphorylates the heat-stable phospho carrier protein at His-15 using PEP as a phosphoryl donor in a reaction that requires EI dimerization and autophosphorylation at His-190. The structure of the full-length protein from Staphylococcus carnosus at 2.5Å reveals an extensive interaction surface between two molecules in adjacent asymmetric units. Structural comparison with related domains indicates that this surface represents the biochemically relevant contact area of dimeric EI. Each monomer has an extended configuration with the phosphohistidine and heat-stable phospho carrier protein-binding domains clearly separated from the C-terminal dimerization and PEP-binding region. The large distance of more than 35Å between the active site His-190 and the PEP binding site suggests that large conformational changes must occur during the process of autophosphorylation, as has been proposed for the structurally related enzyme pyruvate phosphate dikinase. Our structure for the first time offers a framework to analyze a large amount of research in the context of the full-length model.

Received for publication, December 23, 2005 , and in revised form, July 24, 2006.

The atomic coordinates and structure factors (code 2HRO) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Deutsche Forschungsgemeinschaft. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S5.

¹ Both authors contributed equally to this work.

² Present address: Basilea Pharmaceutica AG, Grenzacher Strasse 487, 4005 Basel, Switzerland.

³ To whom correspondence should be addressed. Tel.: 49-6221-387-401; Fax: 49-6221-387-519; E-mail: scheffzek{at}embl.de.

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