5SVV

Structure and kinetics of the LOV domain of ZEITLUPE determine its circadian function in Arabidopsis

5SVV の概要

• エントリーDOI: 10.2210/pdb5svv/pdb
• 関連するPDBエントリー: 5SVG 5SVU 5SVW
• 分子名称: Adagio protein 1, FLAVIN MONONUCLEOTIDE, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: lov, kinetics, pas domain, photoreceptor, circadian clock protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63821.40

構造登録者

Zoltowski, B.,Pudasaini, A. (登録日: 2016-08-07, 公開日: 2017-03-08, 最終更新日: 2023-10-04)

主引用文献

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

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: 28244872
DOI: 10.7554/eLife.21646

実験手法

X-RAY DIFFRACTION (2.101 Å)