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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
Author(s) -
Méchin Marie-Claire,
Bertin Yolande,
Girardeau Jean-Pierre
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(95)00417-8
Subject(s) - structural similarity , protein subunit , protein secondary structure , structural motif , biology , chemistry , peptide sequence , protein structure , biochemistry , stereochemistry , gene
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.