5JYT
NMR structure of foldswitch-stablized KaiB from Thermosynechococcus elongatus
Summary for 5JYT
| Entry DOI | 10.2210/pdb5jyt/pdb |
| Related | 5JYU 5JYV |
| NMR Information | BMRB: 30091 |
| Descriptor | Circadian clock protein KaiB (1 entity in total) |
| Functional Keywords | circadian clock, metamorphic protein, sigaling protein |
| Biological source | Thermosynechococcus elongatus |
| Total number of polymer chains | 1 |
| Total formula weight | 11779.87 |
| Authors | Tseng, R.D.,LiWang, A.L. (deposition date: 2016-05-15, release date: 2017-03-29, Last modification date: 2024-05-15) |
| 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 Cited by 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: 28302851DOI: 10.1126/science.aag2516 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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