Article
Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.
The Journal of biological chemistry - 10 Aug 2007
Aprikian Pavel, Tchesnokova Veronika, Kidd Brian, Yakovenko Olga, Yarov-Yarovoy Vladimir, Trinchina Elena, Vogel Viola, Thomas Wendy, Sokurenko Evgeni
Abstract excerpt
FimH is a mannose-specific adhesin located on the tip of type 1 fimbriae of Escherichia coli that is capable of mediating shear-enhanced bacterial adhesion. FimH consists of a fimbria-associated pilin domain and a mannose-binding lectin domain, with the binding pocket positioned opposite the interdomain interface. By using the yeast two-hybrid system, purified lectin and pilin domains, and docking simulations, we...
Topics
- Adhesins, Escherichia coli
- Cell Adhesion
- Escherichia coli
- Fimbriae Proteins
- Genetic Variation
- Lectins
- Mannose
- Molecular Conformation
- Mutagenesis, Site-Directed
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary