Article
Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli.
Biochemistry - 7 Jan 1997
Frillingos S, Sun J, Gonzalez A, Kaback H R
Abstract excerpt
Using a functional lactose permease mutant devoid of Cys residues (C-less permease), each amino acid residue in putative transmembrane helix II and flanking hydrophilic loops (from Leu34 to Lys74) was replaced individually with Cys. Of the 41 single-Cys mutants, 28 accumulate lactose to > 70% of...
Topics
- Amino Acid Sequence
- Carrier Proteins
- Conserved Sequence
- Cysteine
- Escherichia coli
- Escherichia coli Proteins
- Ethylmaleimide
- Lactose
- Membrane Proteins
- Membrane Transport Proteins
- Molecular Sequence Data
- Monosaccharide Transport Proteins
- Mutagenesis, Site-Directed
- Mutation
- Protein Structure, Secondary
- Symporters