[{"author":[{"full_name":"Tseng, Roger","last_name":"Tseng","first_name":"Roger"},{"first_name":"Nicolette F.","last_name":"Goularte","full_name":"Goularte, Nicolette F."},{"full_name":"Chavan, Archana","first_name":"Archana","last_name":"Chavan"},{"first_name":"Jansen","last_name":"Luu","full_name":"Luu, Jansen"},{"full_name":"Cohen, Susan E.","first_name":"Susan E.","last_name":"Cohen"},{"first_name":"Yong-Gang","last_name":"Chang","full_name":"Chang, Yong-Gang"},{"first_name":"Joel","last_name":"Heisler","full_name":"Heisler, Joel"},{"full_name":"Li, Sheng","first_name":"Sheng","last_name":"Li"},{"id":"6437c950-2a03-11ee-914d-d6476dd7b75c","last_name":"Michael","first_name":"Alicia Kathleen","full_name":"Michael, Alicia Kathleen"},{"first_name":"Sarvind","last_name":"Tripathi","full_name":"Tripathi, Sarvind"},{"first_name":"Susan S.","last_name":"Golden","full_name":"Golden, Susan S."},{"last_name":"LiWang","first_name":"Andy","full_name":"LiWang, Andy"},{"full_name":"Partch, Carrie L.","first_name":"Carrie L.","last_name":"Partch"}],"date_updated":"2024-03-25T12:16:44Z","day":"17","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"American Association for the Advancement of Science","volume":355,"article_processing_charge":"No","date_created":"2024-03-21T07:56:24Z","keyword":["Multidisciplinary"],"language":[{"iso":"eng"}],"page":"1174-1180","type":"journal_article","year":"2017","status":"public","doi":"10.1126/science.aag2516","scopus_import":"1","issue":"6330","extern":"1","abstract":[{"lang":"eng","text":"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."}],"date_published":"2017-03-17T00:00:00Z","month":"03","publication_status":"published","article_type":"original","_id":"15156","quality_controlled":"1","citation":{"chicago":"Tseng, Roger, Nicolette F. Goularte, Archana Chavan, Jansen Luu, Susan E. Cohen, Yong-Gang Chang, Joel Heisler, et al. “Structural Basis of the Day-Night Transition in a Bacterial Circadian Clock.” <i>Science</i>. American Association for the Advancement of Science, 2017. <a href=\"https://doi.org/10.1126/science.aag2516\">https://doi.org/10.1126/science.aag2516</a>.","mla":"Tseng, Roger, et al. “Structural Basis of the Day-Night Transition in a Bacterial Circadian Clock.” <i>Science</i>, vol. 355, no. 6330, American Association for the Advancement of Science, 2017, pp. 1174–80, doi:<a href=\"https://doi.org/10.1126/science.aag2516\">10.1126/science.aag2516</a>.","ista":"Tseng R, Goularte NF, Chavan A, Luu J, Cohen SE, Chang Y-G, Heisler J, Li S, Michael AK, Tripathi S, Golden SS, LiWang A, Partch CL. 2017. Structural basis of the day-night transition in a bacterial circadian clock. Science. 355(6330), 1174–1180.","ama":"Tseng R, Goularte NF, Chavan A, et al. Structural basis of the day-night transition in a bacterial circadian clock. <i>Science</i>. 2017;355(6330):1174-1180. doi:<a href=\"https://doi.org/10.1126/science.aag2516\">10.1126/science.aag2516</a>","apa":"Tseng, R., Goularte, N. F., Chavan, A., Luu, J., Cohen, S. E., Chang, Y.-G., … Partch, C. L. (2017). Structural basis of the day-night transition in a bacterial circadian clock. <i>Science</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/science.aag2516\">https://doi.org/10.1126/science.aag2516</a>","ieee":"R. Tseng <i>et al.</i>, “Structural basis of the day-night transition in a bacterial circadian clock,” <i>Science</i>, vol. 355, no. 6330. American Association for the Advancement of Science, pp. 1174–1180, 2017.","short":"R. Tseng, N.F. Goularte, A. Chavan, J. Luu, S.E. Cohen, Y.-G. Chang, J. Heisler, S. Li, A.K. Michael, S. Tripathi, S.S. Golden, A. LiWang, C.L. Partch, Science 355 (2017) 1174–1180."},"intvolume":"       355","publication_identifier":{"eissn":["1095-9203"],"issn":["0036-8075"]},"publication":"Science","title":"Structural basis of the day-night transition in a bacterial circadian clock","oa_version":"None"}]