Article
Role of the disulfide bond in stabilizing and folding of the fimbrial protein DraE from uropathogenic Escherichia coli.
The Journal of biological chemistry - 29 Sept 2017
Pilipczuk Justyna, Zalewska-Piątek Beata, Bruździak Piotr, Czub Jacek, Wieczór Miłosz, Olszewski Marcin, Wanarska Marta, Nowicki Bogdan, Augustin-Nowacka Danuta, Piątek Rafał
Abstract excerpt
Dr fimbriae are homopolymeric adhesive organelles of uropathogenic Escherichia coli composed of DraE subunits, responsible for the attachment to host cells. These structures are characterized by enormously high stability resulting from the structural properties of an Ig-like fold of DraE. One feature of DraE and other fimbrial subunits that makes them peculiar among Ig-like domain-containing proteins is a...
Topics
- Adhesins, Bacterial
- Amino Acid Sequence
- Amino Acid Substitution
- Bacterial Adhesion
- Cell Line, Tumor
- Conserved Sequence
- Cysteine
- Cystine
- Energy Transfer
- Escherichia coli Proteins