Ontology highlight
ABSTRACT:
SUBMITTER: Keown JR
PROVIDER: S-EPMC3711324 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Keown Jeremy R JR Griffin Michael D W MD Mertens Haydyn D T HD Pearce F Grant FG
The Journal of biological chemistry 20130529 28
Ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase uses the energy from ATP hydrolysis to remove tight binding inhibitors from Rubisco, thus playing a key role in regulating photosynthesis in plants. Although several structures have recently added much needed structural information for different Rubisco activase enzymes, the arrangement of these subunits in solution remains unclear. In this study, we use a variety of techniques to show that Rubisco activase forms a wide range of stru ...[more]