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Pilins of fimbrial adhesins of different member species of enterobacteriaceae are structurally similar to the C‐terminal half of adhesin proteins
Author(s) -
Girardeau Jean-Pierre,
Bertin Yolande
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01340-7
Subject(s) - bacterial adhesin , pilus , enterobacteriaceae , biology , fimbria , microbiology and biotechnology , peptide sequence , genetics , gene , escherichia coli
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.