Article
The N-terminal beta-barrel domain of the Escherichia coli K88 periplasmic chaperone FaeE determines fimbrial subunit recognition and dimerization.
Molecular microbiology - 1 Oct 1996
Mol O, Oudhuis W C, Fokkema H, Oudega B
Abstract excerpt
The K88 periplasmic chaperone FaeE is a homodimer, whereas the K99 chaperone FanE is a monomer. The structural requirements for dimerization of the K88 fimbrial periplasmic chaperone and for fimbrial subunit-binding specificity were investigated by analysis of mutant chaperones. FaeE contains a C-terminal extension of 19 amino acid residues when compared to FanE and most other fimbrial chaperones. A C-terminal...
Topics
- Amino Acid Sequence
- Antigens, Bacterial
- Bacterial Proteins
- Base Sequence
- Dimerization
- Epitopes
- Escherichia coli
- Escherichia coli Proteins
- Fimbriae, Bacterial
- Molecular Chaperones
- Molecular Sequence Data