Structure of a Pilin Monomer from Pseudomonas aeruginosa

DW Keizer, CM Slupsky, M Kalisiak, AM Campbell, MP Crump, PA Sastry, B Hazes, RT Irvin, BD Sykes

Research output: Contribution to journalArticle (Academic Journal)peer-review

99 Citations (Scopus)


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.
Translated title of the contributionStructure of a Pilin Monomer from Pseudomonas aeruginosa
Original languageEnglish
Pages (from-to)24186 - 24193
Number of pages8
JournalJournal of Biological Chemistry
Publication statusPublished - Jun 2001


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