Article
An investigation of cysteine mutants on the cytoplasmic loop X/XI in the melibiose transporter of Escherichia coli by using thiol reagents: implication of structural conservation of charged residues.
Biochemical and biophysical research communications - 8 Aug 2003
Ding Ping Z
Abstract excerpt
The melibiose transporter (Mel B) of Escherichia coli is a cation-coupled (H(+), Li(+), and Na(+)) membrane protein (MW 50 kDa) consisting of 12 transmembrane helices that are connected by periplasmic and cytoplasmic loops, with both the C- and N-ends located on the cytoplasmic side of the membrane. Previous investigations on the largest cytoplasmic loop X/XI indicated that it is a functional re-entrant loop. In...
Topics
- 4-Chloromercuribenzenesulfonate
- Amino Acids
- Animals
- Biological Transport
- Cells, Cultured
- Cysteine
- Escherichia coli Proteins
- Iodoacetic Acid
- Melibiose
- Mesylates
- Mutation
- Protein Structure, Secondary
- Sulfhydryl Reagents
- Symporters