Pilins of fimbrial adhesins of different member species of Enterobacteriaceae are structurally similar to the C-terminal half of adhesin proteins.
The structural relatedness of pilins and the C-terminal half of adhesin proteins in different member species of Enterobacteriaceae was deduced from their two-dimensional sequence analysis using the hydrophobic cluster analysis (HCA) and secondary structure predictions from the profile network Hei-Delberg program (PHD). Despite a large evolutionary distance between the two protein families, we show that pilins and the C-terminal domain of adhesins have a similar folding that can serve as modules for pilus assembly.
Girardeau
J P
JP
Laboratoire de Microbiologie, INRA, Centre de Recherches de Clermont-Ferrand-Theix, Saint-Genès-Champanelle, France.
Bertin
Y
Y
D018829:Adhesins, Bacterial / Q000737:chemistry*; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004755:Enterobacteriaceae / Q000737:chemistry*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D036781:Fimbriae Proteins