Article
Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering.
Scientific reports - 18 Oct 2016
Sugiyama Masaaki, Yagi Hirokazu, Ishii Kentaro, Porcar Lionel, Martel Anne, Oyama Katsuaki, Noda Masanori, Yunoki Yasuhiro, Murakami Reiko, Inoue Rintaro, Sato Nobuhiro, Oba Yojiro, Terauchi Kazuki, Uchiyama Susumu, Kato Koichi
Abstract excerpt
The molecular machinery of the cyanobacterial circadian clock consists of three proteins: KaiA, KaiB, and KaiC. Through interactions among the three Kai proteins, the phosphorylation states of KaiC generate circadian oscillations in vitro in the presence of ATP. Here, we characterized the complex formation between KaiB and KaiC using a phospho-mimicking mutant of KaiC, which had an aspartate substitution at the...
Topics
- Bacterial Proteins
- Circadian Clocks
- Circadian Rhythm Signaling Peptides and Proteins
- Crystallography, X-Ray
- Multiprotein Complexes
- Mutation
- Phosphorylation
- Phosphotransferases
- Protein Binding