Hydrophobic cluster analysis and secondary structure predictions revealed that major and minor structural subunits of K88-related adhesins of Escherichia coli share a common overall fold and differ structurally from other fimbrial subunits.
The structural relatedness of K88-related major and minor subunits was deduced from their sequences by hydrophobic cluster analysis (HCA) and secondary structure predictions produced by the profile neural network prediction program (PHD) on multiple sequence alignments. Although the weak residue identity between major and minor subunits is evidence of a high evolutionary distance, an overall structural similarity was observed In addition, clear amphipathic conformations were conserved in predicted secondary structure. On the basis of this predicted structural similarity, a schematic 2D model of ClpG subunit was developed.
Méchin
M C
MC
Laboratoire de Microbiologie, INRA, Centre de Recherches de Clermont-Ferrand-Theix, Saint-Genes-Champanelle, France.
Bertin
Y
Y
Girardeau
J P
JP
D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000737:chemistry; D000954:Antigens, Surface / Q000737:chemistry*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D000942:Antigens, Bacterial; D000954:Antigens, Surface; D029968:Escherichia coli Proteins; C026888:K88 antigen, E coli; D036781:Fimbriae Proteins