5JWR

Crystal structure of foldswitch-stabilized KaiB in complex with the N-terminal CI domain of KaiC and a dimer of KaiA C-terminal domains from Thermosynechococcus elongatus

Summary for 5JWR

• Entry DOI: 10.2210/pdb5jwr/pdb
• Related: 5JWO 5JWQ
• Descriptor: Circadian clock protein kinase KaiC, Circadian clock protein KaiB, Circadian clock protein KaiA, ... (5 entities in total)
• Functional Keywords: transcription regulator, foldswitch
• Biological source: Thermosynechococcus elongatus; More
• Total number of polymer chains: 8
• Total formula weight: 146879.33

Authors

Tseng, R.,Goularte, N.F.,Chavan, A.,Luu, J.,Chang, Y.G.,Heilser, J.,Tripathi, S.,LiWang, A.,Partch, C.L. (deposition date: 2016-05-12, release date: 2017-03-29, Last modification date: 2024-03-06)

Primary citation

Tseng, R.,Goularte, N.F.,Chavan, A.,Luu, J.,Cohen, S.E.,Chang, Y.G.,Heisler, J.,Li, S.,Michael, A.K.,Tripathi, S.,Golden, S.S.,LiWang, A.,Partch, C.L.
Structural basis of the day-night transition in a bacterial circadian clock.
Science, 355:1174-1180, 2017

PubMed 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.

PubMed: 28302851
DOI: 10.1126/science.aag2516

Experimental method

X-RAY DIFFRACTION (2.61 Å)