6QTT

Crystal structure of an Arabidopsis WD40 domain in complex with a transcription factor homolog

6QTT の概要

• エントリーDOI: 10.2210/pdb6qtt/pdb
• 分子名称: E3 ubiquitin-protein ligase COP1, Transcription factor HY5-like, MALONATE ION, ... (5 entities in total)
• 機能のキーワード: complex, plant protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38637.21

構造登録者

Hothorn, M.,Lau, K. (登録日: 2019-02-25, 公開日: 2019-07-10, 最終更新日: 2024-10-09)

主引用文献

Lau, K.,Podolec, R.,Chappuis, R.,Ulm, R.,Hothorn, M.
Plant photoreceptors and their signaling components compete for COP1 binding via VP peptide motifs.
Embo J., 38:e102140-e102140, 2019

PubMed Abstract: Plants sense different parts of the sun's light spectrum using distinct photoreceptors, which signal through the E3 ubiquitin ligase COP1. Here, we analyze why many COP1-interacting transcription factors and photoreceptors harbor sequence-divergent Val-Pro (VP) motifs that bind COP1 with different binding affinities. Crystal structures of the VP motifs of the UV-B photoreceptor UVR8 and the transcription factor HY5 in complex with COP1, quantitative binding assays, and reverse genetic experiments together suggest that UVR8 and HY5 compete for COP1. Photoactivation of UVR8 leads to high-affinity cooperative binding of its VP motif and its photosensing core to COP1, preventing COP1 binding to its substrate HY5. UVR8-VP motif chimeras suggest that UV-B signaling specificity resides in the UVR8 photoreceptor core. Different COP1-VP peptide motif complexes highlight sequence fingerprints required for COP1 targeting. The blue-light photoreceptors CRY1 and CRY2 also compete with transcription factors for COP1 binding using similar VP motifs. Thus, our work reveals that different photoreceptors and their signaling components compete for COP1 via a conserved mechanism to control different light signaling cascades.

PubMed: 31304983
DOI: 10.15252/embj.2019102140

実験手法

X-RAY DIFFRACTION (1.51 Å)