Article
Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9.
Microbiology (Reading, England) - 1 Sept 1997
-Schneider Carole Garinot, Penfold Christopher N, Moore Geoffrey R, Kleanthous Colin, James Richard
Abstract excerpt
E colicins are plasmid-coded, protein antibiotics which bind to the BtuB outer membrane receptor of Escherichia coli cells and are then translocated either to the outer surface of the cytoplasmic membrane in the case of the pore-forming colicin E1, or to the cytoplasm in the case of the enzymic c...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Bacterial Toxins
- Binding Sites
- Biological Transport, Active
- Colicins
- Endonucleases
- Escherichia coli
- Escherichia coli Proteins
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Phenotype
- Restriction Mapping
- Sequence Homology, Amino Acid