4DNU

Crystal structure of the W285A mutant of UVB-resistance protein UVR8

Summary for 4DNU

• Entry DOI: 10.2210/pdb4dnu/pdb
• Related: 4DNV 4DNW
• Descriptor: AT5g63860/MGI19_6 (2 entities in total)
• Functional Keywords: wd40 repeats, uv-b perception, cop1, gene regulation
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Nucleus: Q9FN03
• Total number of polymer chains: 1
• Total formula weight: 40241.84

Authors

Wu, D.,Hu, Q.,Yan, Z.,Chen, W.,Yan, C.,Zhang, J.,Wang, J.,Shi, Y. (deposition date: 2012-02-09, release date: 2012-03-07, Last modification date: 2024-10-30)

Primary citation

Wu, D.,Hu, Q.,Yan, Z.,Chen, W.,Yan, C.,Huang, X.,Zhang, J.,Yang, P.,Deng, H.,Wang, J.,Deng, X.,Shi, Y.
Structural basis of ultraviolet-B perception by UVR8.
Nature, 484:214-219, 2012

PubMed Abstract: The Arabidopsis thaliana protein UVR8 is a photoreceptor for ultraviolet-B. Upon ultraviolet-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, which triggers a signalling pathway for ultraviolet protection. The mechanism by which UVR8 senses ultraviolet-B remains largely unknown. Here we report the crystal structure of UVR8 at 1.8 Å resolution, revealing a symmetric homodimer of seven-bladed β-propeller that is devoid of any external cofactor as the chromophore. Arginine residues that stabilize the homodimeric interface, principally Arg 286 and Arg 338, make elaborate intramolecular cation-π interactions with surrounding tryptophan amino acids. Two of these tryptophans, Trp 285 and Trp 233, collectively serve as the ultraviolet-B chromophore. Our structural and biochemical analyses identify the molecular mechanism for UVR8-mediated ultraviolet-B perception, in which ultraviolet-B radiation results in destabilization of the intramolecular cation-π interactions, causing disruption of the critical intermolecular hydrogen bonds mediated by Arg 286 and Arg 338 and subsequent dissociation of the UVR8 homodimer.

PubMed: 22388820
DOI: 10.1038/nature10931

Experimental method

X-RAY DIFFRACTION (1.764 Å)