@article{15156,
  abstract     = {Circadian clocks are ubiquitous timing systems that induce rhythms of biological activities in synchrony with night and day. In cyanobacteria, timing is generated by a posttranslational clock consisting of KaiA, KaiB, and KaiC proteins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control gene expression. Here, we describe crystal and nuclear magnetic resonance structures of KaiB-KaiC,KaiA-KaiB-KaiC, and CikA-KaiB complexes. They reveal how the metamorphic properties of KaiB, a protein that adopts two distinct folds, and the post–adenosine triphosphate hydrolysis state of KaiC create a hub around which nighttime signaling events revolve, including inactivation of KaiA and reciprocal regulation of the mutually antagonistic signaling proteins, SasA and CikA.},
  author       = {Tseng, Roger and Goularte, Nicolette F. and Chavan, Archana and Luu, Jansen and Cohen, Susan E. and Chang, Yong-Gang and Heisler, Joel and Li, Sheng and Michael, Alicia Kathleen and Tripathi, Sarvind and Golden, Susan S. and LiWang, Andy and Partch, Carrie L.},
  issn         = {1095-9203},
  journal      = {Science},
  keywords     = {Multidisciplinary},
  number       = {6330},
  pages        = {1174--1180},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Structural basis of the day-night transition in a bacterial circadian clock}},
  doi          = {10.1126/science.aag2516},
  volume       = {355},
  year         = {2017},
}