Article
Conformational changes in the Escherichia coli ATP synthase (ECF1F0) monitored by nucleotide-dependent differences in the reactivity of Cys-87 of the gamma subunit in the mutant betaGlu-381 --> Ala.
The Journal of biological chemistry - 26 Jul 1996
Feng Z, Aggeler R, Haughton M A, Capaldi R A
Abstract excerpt
Cys-87, one of two intrinsic cysteines of the gamma subunit of the Escherichia coli ATP synthase (ECF1F0), is in a short segment of this subunit that binds to the bottom domain of a beta subunit close to a glutamate (Glu-381). Cys-87 was unreactive to maleimides under all conditions in wild-type...
Topics
- Base Sequence
- Cysteine
- Escherichia coli
- Maleimides
- Molecular Sequence Data
- Mutation
- Nucleotides
- Protein Conformation
- Proton-Translocating ATPases