2004年7月
Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein
NATURE STRUCTURAL & MOLECULAR BIOLOGY
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 11
- 号
- 7
- 開始ページ
- 623
- 終了ページ
- 631
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/nsmb781
- 出版者・発行元
- NATURE PUBLISHING GROUP
KaiA, KaiB and KaiC constitute the circadian clock machinery in cyanobacteria, and KaiA activates kaiBC expression whereas KaiC represses it. Here we show that KaiA is composed of three functional domains, the N-terminal amplitude-amplifier domain, the central period-adjuster domain and the C-terminal clock-oscillator domain. The C-terminal domain is responsible for dimer formation, binding to KaiC, enhancing KaiC phosphorylation and generating the circadian oscillations. The X-ray crystal structure at a resolution of 1.8 Angstrom of the C-terminal clock-oscillator domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 shows that residue His270, located at the center of a KaiA dimer concavity, is essential to KaiA function. KaiA binding to KaiC probably occurs via the concave surface. On the basis of the structure, we predict the structural roles of the residues that affect circadian oscillations.
- リンク情報
- ID情報
-
- DOI : 10.1038/nsmb781
- ISSN : 1545-9985
- Web of Science ID : WOS:000222274100011