Article
The penultimate tyrosine residue of the K99 fibrillar subunit is essential for stability of the protein and its interaction with the periplasmic carrier protein.
FEMS microbiology letters - 15 Jan 1990
Simons B L, Rathman P, Malij C R, Oudega B, de Graaf F K
Abstract excerpt
The role of the penultimate and conserved tyrosine residue of the K99 major fibrillar subunit (FanC) in fibrillae biosynthesis and functioning was investigated. By using oligonucleotide-directed in vitro mutagenesis the TAT codon of tyrosine-158 of fanC was changed into a TAG stop codon. The mutant fanC gene encoded a truncated major subunit lacking the two carboxyl-terminal amino acid residues. Furthermore, the...
Topics
- Amino Acid Sequence
- Antigens, Surface
- Bacterial Proteins
- Bacterial Toxins
- Binding Sites
- Carrier Proteins
- Chromosome Mapping
- Escherichia coli
- Fimbriae, Bacterial
- Molecular Sequence Data