Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm.

@article{Hitomi2005TetramericAO,
  title={Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm.},
  author={Kenichi Hitomi and Tokitaka Oyama and Seungil Han and Andrew S. Arvai and Elizabeth D. Getzoff},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 19},
  pages={19127-35}
}
Cyanobacteria are among the simplest organisms that show daily rhythmicity. Their circadian rhythms consist of the localization, interaction, and accumulation of various proteins, including KaiA, KaiB, KaiC, and SasA. We have determined the 1.9-angstroms resolution crystallographic structure of the cyanobacterial KaiB clock protein from Synechocystis sp. PCC6803. This homotetrameric structure reveals a novel KaiB interface for protein-protein interaction; the protruding hydrophobic helix-turn… CONTINUE READING

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