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J. Biol. Chem., Vol. 280, Issue 48, 40252-40260, December 2, 2005

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Structure of the Bundle-forming Pilus from Enteropathogenic Escherichia coli^*

Stéphanie Ramboarina, Paula J. Fernandes¶, Sarah Daniell, Suhail Islam, Pete Simpson, Gad Frankel, Frank Booy, Michael S. Donnenberg¶1, and Stephen Matthews2

From the Department of Biological Sciences, Wolfson Laboratory and the Center for Structural Biology, Imperial College London SW7 2AZ, United Kingdom and the ^¶Division of Infectious Diseases, School of Medicine, University of Maryland, Baltimore, Maryland 21201

Bundle-forming pili (BFP) are essential for the full virulence of enteropathogenic Escherichia coli (EPEC) because they are required for localized adherence to epithelial cells and auto-aggregation. We report the high resolution structure of bundlin, the monomer of BFP, solved by NMR. The structure reveals a new variation in the topology of type IVb pilins with significant differences in the composition and relative orientation of elements of secondary structure. In addition, the structural parameters of native BFP filaments were determined by electron microscopy after negative staining. The solution structure of bundlin was assembled according to these helical parameters to provide a plausible atomic resolution model for the BFP filament. We show that EPEC and Vibriocholerae type IVb pili display distinct differences in their monomer subunits consistent with data showing that bundlin and TcpA cannot complement each other, but assemble into filaments with similar helical organization.

Received for publication, July 25, 2005 , and in revised form, September 15, 2005.

The atomic coordinates and structure factors (code 1zwt) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

NMR assignments and restraints have been deposited in BioMagResBank under the accession code 6003.

^* This work was supported by The Wellcome Trust. 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.

¹ To whom correspondence may be addressed. E-mail: mdonnenb{at}umaryland.edu.

² To whom correspondence may be addressed. E-mail: s.j.matthews{at}imperial.ac.uk.

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