Hydrophobic cluster analysis and secondary structure predictions revealed that major and minor structural subunits of K88-related adhesins ofEscherichia colishare a common overall fold and differ structurally from other fimbrial subunits
- 15 May 1995
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 364 (3), 319-324
- https://doi.org/10.1016/0014-5793(95)00417-8
Abstract
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 developedKeywords
This publication has 25 references indexed in Scilit:
- Pilins of fimbrial adhesins of different member species of enterobacteriaceae are structurally similar to the C-terminal half of adhesin proteinsFEBS Letters, 1995
- Conservation of amphipathic conformations in multiple protein structural alignmentsProtein Engineering, Design and Selection, 1994
- Structural Basis of Pilus Subunit Recognition by the PaPd ChaperoneScience, 1993
- Amino acid sequence similarities between low molecular weight endo‐1,4‐β‐xylanases and family H cellulases revealed by clustering analysisFEBS Letters, 1993
- Analysis of insertions/deletions in protein structuresJournal of Molecular Biology, 1992
- Characterization of the antigenic and adhesive properties of FaeG, the major subunit of K88 fimbriaeMolecular Microbiology, 1992
- Structure-function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coliMolecular Microbiology, 1991
- Structure and function of peripiasmic chaperone‐like proteins involved in the biosynthesis of K88 and K99 fimbriae in enterotoxigenic Escherichia coliMolecular Microbiology, 1991
- Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequencesFEBS Letters, 1987
- The nucleotide sequence of the protein subunit of the K88ac fimbriae of porcine enterotoxigenicEscherichia coliFEMS Microbiology Letters, 1984