Article
In vivo affinity label of a protein expressed in Escherichia coli. Coenzyme A occupied the AT(D)P binding site of the mutant F1-ATPase beta subunit (Y307C) through a disulfide bond.
FEBS letters - 27 Dec 1993
Odaka M, Kiribuchi K, Allison W S, Yoshida M
Abstract excerpt
When Tyr-307 of the beta subunit of F1-ATPase from a thermophilic Bacillus strain PS3 is replaced by cysteine and expressed in Escherichia coli cells, about a half population of the mutant beta subunit are labeled by Coenzyme A at Cys-307 through a disulfide bond which is cleavable by reducing tr...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Affinity Labels
- Bacillus
- Bacterial Proteins
- Binding Sites
- Chromatography, High Pressure Liquid
- Cloning, Molecular
- Coenzyme A
- Cysteine
- Disulfides
- Enzyme Activation
- Escherichia coli
- Mutation
- Proton-Translocating ATPases
- Recombinant Proteins
- Spectrophotometry, Ultraviolet