Article
Structures of KaiC circadian clock mutant proteins: a new phosphorylation site at T426 and mechanisms of kinase, ATPase and phosphatase.
PloS one - 26 Nov 2009
Pattanayek Rekha, Mori Tetsuya, Xu Yao, Pattanayek Sabuj, Johnson Carl H, Egli Martin
Abstract excerpt
BACKGROUND: The circadian clock of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro by three proteins, KaiA, KaiB and KaiC. Homo-hexameric KaiC displays kinase, phosphatase and ATPase activities; KaiA enhances KaiC phosphorylation and KaiB antagonizes KaiA. Phosphorylation...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Bacterial Proteins
- Binding Sites
- Catalytic Domain
- Circadian Rhythm
- Circadian Rhythm Signaling Peptides and Proteins
- Crystallography, X-Ray
- Gene Expression Regulation, Bacterial
- Models, Biological
- Mutation
- Phosphoric Monoester Hydrolases
- Phosphorylation