5SVG
Structure and kinetics of the LOV domain of ZEITLUPE determine its circadian function in Arabidopsis
Summary for 5SVG
| Entry DOI | 10.2210/pdb5svg/pdb |
| Related | 5SVU 5SVV 5SVW |
| Descriptor | Adagio protein 1, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | lov, kinetics, pas domain, photoreceptor, circadian clock protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 63003.40 |
| Authors | Zoltowski, B.,Pudasaini, A. (deposition date: 2016-08-05, release date: 2017-03-08, Last modification date: 2023-10-04) |
| Primary citation | Pudasaini, A.,Shim, J.S.,Song, Y.H.,Shi, H.,Kiba, T.,Somers, D.E.,Imaizumi, T.,Zoltowski, B.D. Kinetics of the LOV domain of ZEITLUPE determine its circadian function inArabidopsis. Elife, 6:-, 2017 Cited by PubMed Abstract: A LOV (Light, Oxygen, or Voltage) domain containing blue-light photoreceptor ZEITLUPE (ZTL) directs circadian timing by degrading clock proteins in plants. Functions hinge upon allosteric differences coupled to the ZTL photocycle; however, structural and kinetic information was unavailable. Herein, we tune the ZTL photocycle over two orders of magnitude. These variants reveal that ZTL complexes with targets independent of light, but dictates enhanced protein degradation in the dark. In vivo experiments definitively show photocycle kinetics dictate the rate of clock component degradation, thereby impacting circadian period. Structural studies demonstrate that photocycle dependent activation of ZTL depends on an unusual dark-state conformation of ZTL. Crystal structures of ZTL LOV domain confirm delineation of structural and kinetic mechanisms and identify an evolutionarily selected allosteric hinge differentiating modes of PAS/LOV signal transduction. The combined biochemical, genetic and structural studies provide new mechanisms indicating how PAS/LOV proteins integrate environmental variables in complex networks. PubMed: 28244872DOI: 10.7554/eLife.21646 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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