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J. Biol. Chem., Vol. 276, Issue 26, 24186-24193, June 29, 2001

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Structure of a Pilin Monomer from Pseudomonas aeruginosa
IMPLICATIONS FOR THE ASSEMBLY OF PILI^*

David W. Keizer, Carolyn M. Slupsky, Michal Kalisiak^§, A. Patricia Campbell^¶, Matthew P. Crump, Parimi A. Sastry^§, Bart Hazes^§, Randall T. Irvin^§, and Brian D. Sykes^**

From the  Protein Engineering Network Centres of Excellence (PENCE), 713 Heritage Medical Research Centre, University of Alberta, Edmonton, Alberta T6G 2S2, Canada, the ^§ Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada, the  Department of Biochemistry, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, United Kingdom, and the ^¶ Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, Washington 98195

Type IV pilin monomers assemble to form fibers called pili that are required for a variety of bacterial functions. Pilin monomers oligomerize due to the interaction of part of their hydrophobic N-terminal -helix. Engineering of a truncated pilin from Pseudomonas aeruginosa strain K122-4, where the first 28 residues are removed from the N terminus, yields a soluble, monomeric protein. This truncated pilin is shown to bind to its receptor and to decrease morbidity and mortality in mice upon administration 15 min before challenge with a heterologous strain of Pseudomonas. The structure of this truncated pilin reveals an -helix at the N terminus that lies across a 4-stranded antiparallel -sheet. A model for a pilus is proposed that takes into account both electrostatic and hydrophobic interactions of pilin subunits as well as previously published x-ray fiber diffraction data. Our model indicates that DNA or RNA cannot pass through the center of the pilus, however, the possibility exists for small organic molecules to pass through indicating a potential mechanism for signal transduction.

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

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