Structural basis of ultraviolet-B perception by UVR8

Di Wu, Qi Hu, Zhen Yan, Wen Chen, Chuangye Yan, Xi Huang, Jing Zhang, Panyu Yang, Haiteng Deng, Jiawei Wang, XingWang Deng and Yigong Shi ()
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Di Wu: Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Qi Hu: Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Zhen Yan: Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Wen Chen: College of Life Sciences, Peking University
Chuangye Yan: State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Xi Huang: College of Life Sciences, Peking University
Jing Zhang: Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Panyu Yang: College of Life Sciences, Peking University
Haiteng Deng: Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Jiawei Wang: State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
XingWang Deng: College of Life Sciences, Peking University
Yigong Shi: Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University

Nature, 2012, vol. 484, issue 7393, 214-219

Abstract: 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.

Date: 2012
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DOI: 10.1038/nature10931

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