Hazes et al., J. Mol. Biol. 299, p1005-17 (2000)
Depicted is the 1.63 Å crystal structure of truncated PAK pilin. The molecule is formed by a central alpha helix (blue) packed onto a four-stranded antiparallel beta sheet, the major sheet (green). These structural elements are shared by all type IV pilin molecules. The small beta-sheet, the minor sheet (yellow), is not found in Neisseria gonorrhoeae pilin which, instead, has an O-linked carbohydrate moiety that occupies the same space. The C-terminal end of the molecule (shown in red) forms a disulphide-bonded loop which is present in all type IV pilins. It is this part of the molecule that has been shown to adhere to human cell surface receptors; in particular the glycolipid asialo-GM1. Our research goal is to understand the molecular basis for receptor recognition by a variety of P. aeruginosa strains in the hope to design new therapeutics that can block receptor binding and thereby prevent disease.