Article
Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin.
Proceedings of the National Academy of Sciences of the United States of America - 11 Apr 1995
Sano T, Cantor C R
Abstract excerpt
In natural streptavidin, tryptophan 120 of each subunit makes contacts with the biotin bound by an adjacent subunit through the dimer-dimer interface. To understand quantitatively the role of tryptophan 120 and its intersubunit communication in the properties of streptavidin, a streptavidin mutant in which tryptophan 120 is converted to phenylalanine was produced and characterized. The streptavidin mutant forms a...
Topics
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Biotin
- Dialysis
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Denaturation