Article
Structural analysis of the regulatory dithiol-containing domain of the chloroplast ATP synthase gamma subunit.
The Journal of biological chemistry - 13 Oct 2006
Samra Hardeep S, Gao Fei, He Feng, Hoang Etter, Chen Zugen, Gegenheimer Peter A, Berrie Cindy L, Richter Mark L
Abstract excerpt
The gamma subunit of the F1 portion of the chloroplast ATP synthase contains a critically placed dithiol that provides a redox switch converting the enzyme from a latent to an active ATPase. The switch prevents depletion of intracellular ATP pools in the dark when photophosphorylation is inactive. The dithiol is located in a special regulatory segment of about 40 amino acids that is absent from the gamma subunits...
Topics
- Alanine
- Chloroplast Proton-Translocating ATPases
- Chloroplasts
- Gene Deletion
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Protein Structure, Tertiary
- Proton-Translocating ATPases
- Spinacia oleracea