7VGG

Cryo-EM structure of Ultraviolet-B activated UVR8 in complex with COP1

Summary for 7VGG

• Entry DOI: 10.2210/pdb7vgg/pdb
• EMDB information: 31968
• Descriptor: E3 ubiquitin-protein ligase COP1, Ultraviolet-B receptor UVR8 (2 entities in total)
• Functional Keywords: cop1, uvr8, signaling protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 2
• Total formula weight: 129957.69

Authors

Wang, Y.D.,Wang, L.X.,Guan, Z.Y.,Yin, P. (deposition date: 2021-09-16, release date: 2022-05-04, Last modification date: 2024-06-19)

Primary citation

Wang, Y.,Wang, L.,Guan, Z.,Chang, H.,Ma, L.,Shen, C.,Qiu, L.,Yan, J.,Zhang, D.,Li, J.,Deng, X.W.,Yin, P.
Structural insight into UV-B-activated UVR8 bound to COP1.
Sci Adv, 8:eabn3337-eabn3337, 2022

PubMed Abstract: The CONSTITUTIVE PHOTOMORPHOGENIC 1-SUPPRESSOR OF PHYA-105 (COP1-SPA) complex is a central repressor of photomorphogenesis. This complex acts as an E3 ubiquitin ligase downstream of various light signaling transduced from multiple photoreceptors in plants. How the COP1-SPA activity is regulated by divergent light-signaling pathways remains largely elusive. Here, we reproduced the regulation pathway of COP1-SPA in ultraviolet-B (UV-B) signaling in vitro and determined the cryo-electron microscopy structure of UV-B receptor UVR8 in complex with COP1. The complex formation is mediated by two-interface interactions between UV-B-activated UVR8 and COP1. Both interfaces are essential for the competitive binding of UVR8 against the signaling hub component HY5 to the COP1-SPA complex. We also show that RUP2 dissociates UVR8 from the COP1-SPA4-UVR8 complex and facilitates its redimerization. Our results support a UV-B signaling model that the COP1-SPA activity is repressed by UV-B-activated UVR8 and derepressed by RUP2, owing to competitive binding, and provide a framework for studying the regulatory roles of distinct photoreceptors on photomorphogenesis.

PubMed: 35442727
DOI: 10.1126/sciadv.abn3337

Experimental method

ELECTRON MICROSCOPY (3.1 Å)