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,

338 and subsequent dissociation of the UVR8 homodimer. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS

Access through your institution Subscribe to this journal Receive 51 print issues and online access $199.00 per year only $3.90 per issue Learn more Buy this article * Purchase on

SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about

institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS A LEAP IN QUANTUM EFFICIENCY THROUGH LIGHT HARVESTING IN PHOTORECEPTOR UVR8

Article Open access 28 August 2020 DYNAMICS AND MECHANISM OF DIMER DISSOCIATION OF PHOTORECEPTOR UVR8 Article Open access 10 January 2022 PHOSPHORYLATION OF ARABIDOPSIS UVR8 PHOTORECEPTOR

MODULATES PROTEIN INTERACTIONS AND RESPONSES TO UV-B RADIATION Article Open access 09 February 2024 ACCESSION CODES PRIMARY ACCESSIONS PROTEIN DATA BANK * 4DNU * 4DNV * 4DNW DATA DEPOSITS

The atomic coordinates and structure factor files of UVR8 wild type, W285A and W285F have been deposited in the Protein Data Bank under accession codes 4DNW, 4DNU and 4DNV, respectively.

REFERENCES * Falciatore, A. & Bowler, C. The evolution and function of blue and red light photoreceptors. _Curr. Top. Dev. Biol._ 68, 317–350 (2005) CAS  Google Scholar  * van der

Linden, A. M. et al. Genome-wide analysis of light- and temperature-entrained circadian transcripts in _Caenorhabditis elegans_. _PLoS Biol._ 8, e1000503 (2010) Google Scholar  * Fogle, K.

J., Parson, K. G., Dahm, N. A. & Holmes, T. C. CRYPTOCHROME is a blue-light sensor that regulates neuronal firing rate. _Science_ 331, 1409–1413 (2011) CAS  Google Scholar  * Jiao, Y.,

Lau, O. S. & Deng, X. W. Light-regulated transcriptional networks in higher plants. _Nature Rev. Genet._ 8, 217–230 (2007) CAS  Google Scholar  * Kami, C., Lorrain, S., Hornitschek, P.

& Fankhauser, C. Light-regulated plant growth and development. _Curr. Top. Dev. Biol._ 91, 29–66 (2010) CAS  Google Scholar  * Quail, P. H. Phytochrome photosensory signalling networks.

_Nature Rev. Mol. Cell Biol._ 3, 85–93 (2002) CAS  Google Scholar  * Briggs, W. R. & Christie, J. M. Phototropins 1 and 2: versatile plant blue-light receptors. _Trends Plant Sci._ 7,

204–210 (2002) CAS  Google Scholar  * Chaves, I. et al. The cryptochromes: blue light photoreceptors in plants and animals. _Annu. Rev. Plant Biol._ 62, 335–364 (2011) CAS  Google Scholar  *

Cashmore, A. R., Jarillo, J. A., Wu, Y. J. & Liu, D. Cryptochromes: blue light receptors for plants and animals. _Science_ 284, 760–765 (1999) CAS  Google Scholar  * Christie, J. M.

Phototropin blue-light receptors. _Annu. Rev. Plant Biol._ 58, 21–45 (2007) CAS  Google Scholar  * Liu, H., Liu, B., Zhao, C., Pepper, M. & Lin, C. The action mechanisms of plant

cryptochromes. _Trends Plant Sci._ 16, 684–691 (2011) CAS  Google Scholar  * Rizzini, L. et al. Perception of UV-B by the _Arabidopsis_ UVR8 protein. _Science_ 332, 103–106 (2011) CAS 

Google Scholar  * Möglich, A., Yang, X., Ayers, R. A. & Moffat, K. Structure and function of plant photoreceptors. _Annu. Rev. Plant Biol._ 61, 21–47 (2010) Google Scholar  *

Kliebenstein, D. J., Lim, J. E., Landry, L. G. & Last, R. L. _Arabidopsis_ UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human

regulator of chromatin condensation 1. _Plant Physiol._ 130, 234–243 (2002) CAS  Google Scholar  * Brown, B. A. et al. A UV-B-specific signaling component orchestrates plant UV protection.

_Proc. Natl Acad. Sci. USA_ 102, 18225–18230 (2005) CAS  Google Scholar  * Brown, B. A. & Jenkins, G. I. UV-B signaling pathways with different fluence-rate response profiles are

distinguished in mature _Arabidopsis_ leaf tissue by requirement for UVR8, HY5, and HYH. _Plant Physiol._ 146, 576–588 (2008) CAS  Google Scholar  * Kaiserli, E. & Jenkins, G. I. UV-B

promotes rapid nuclear translocation of the _Arabidopsis_ UV-B specific signaling component UVR8 and activates its function in the nucleus. _Plant Cell_ 19, 2662–2673 (2007) CAS  Google

Scholar  * Li, D. & Roberts, R. WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. _Cell. Mol. Life Sci._ 58, 2085–2097 (2001)

CAS  Google Scholar  * Wall, M. A. et al. The structure of the G protein heterotrimer Giα1β1γ2 . _Cell_ 83, 1047–1058 (1995) CAS  Google Scholar  * Renault, L. et al. The 1.7 Å crystal

structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. _Nature_ 392, 97–101 (1998) CAS  Google Scholar  * Gallivan, J. P. & Dougherty, D. A.

Cation–π interactions in structural biology. _Proc. Natl Acad. Sci. USA_ 96, 9459–9464 (1999) CAS  Google Scholar  * Gallivan, J. P. & Dougherty, D. A. A computational study of cation−π

interactions vs salt bridges in aqueous media: implications for protein engineering. _J. Am. Chem. Soc._ 122, 870–874 (2000) CAS  Google Scholar  * Dougherty, D. A. Cation−π interactions

involving aromatic amino acids. _J. Nutr._ 137, 1504S–1508S (2007) CAS  Google Scholar  * Sinnokrot, M. O., Valeev, E. F. & Sherrill, C. D. Estimates of the _ab initio_ limit for π–π

interactions: the benzene dimer. _J. Am. Chem. Soc._ 124, 10887–10893 (2002) CAS  Google Scholar  * Wagner, J. R., Brunzelle, J. S., Forest, K. T. & Vierstra, R. D. A light-sensing knot

revealed by the structure of the chromophore-binding domain of phytochrome. _Nature_ 438, 325–331 (2005) CAS  Google Scholar  * Ulijasz, A. T. et al. Structural basis for the photoconversion

of a phytochrome to the activated Pfr form. _Nature_ 463, 250–254 (2010) CAS  Google Scholar  * Brudler, R. et al. Identification of a new cryptochrome class. Structure, function, and

evolution. _Mol. Cell_ 11, 59–67 (2003) CAS  Google Scholar  * Brautigam, C. A. et al. Structure of the photolyase-like domain of cryptochrome 1 from _Arabidopsis_ _thaliana_. _Proc. Natl

Acad. Sci. USA_ 101, 12142–12147 (2004) CAS  Google Scholar  * Crosson, S. & Moffat, K. Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal

transduction. _Proc. Natl Acad. Sci. USA_ 98, 2995–3000 (2001) CAS  Google Scholar  * Crosson, S. & Moffat, K. Photoexcited structure of a plant photoreceptor domain reveals a

light-driven molecular switch. _Plant Cell_ 14, 1067–1075 (2002) CAS  Google Scholar  * Yu, H. T., Colucci, W. J., McLaughlin, M. L. & Barkley, M. D. Fluorescence quenching in indoles by

excited-state proton transfer. _J. Am. Chem. Soc._ 114, 8449–8454 (1992) CAS  Google Scholar  * Christie, J. M. et al. Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption

of cross-dimer salt bridges. _Science_http://dx.doi.org/10.1126/science.1218091 (9 February 2012) * Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in

oscillation mode. _Methods Enzymol._ 276, 307–326 (1997) CAS  Google Scholar  * Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. _Acta Crystallogr.

D_ 50, 760–763 (1994) * Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. _Acta Crystallogr. D_ 58, 1772–1779 (2002) Google Scholar  * Cowtan, K. The Buccaneer

software for automated model building. _Acta Crystallogr. D_ 62, 1002–1011 (2006) Google Scholar  * Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. _Acta

Crystallogr. D_ 60, 2126–2132 (2004) Google Scholar  * Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. _Acta Crystallogr. D_ 58,

1948–1954 (2002) Google Scholar  * McCoy, A. J. et al. Phaser crystallographic software. _J. Appl. Cryst._ 40, 658–674 (2007) CAS  Google Scholar  * DeLano, W. L. The PyMOL Molecular

Graphics System. http://www.pymol.org (2002) Download references ACKNOWLEDGEMENTS We thank J. He and S. Huang at SSRF, and K. Hasegawa and T. Kumasaka at the SPring-8 beamline BL41XU, for

assistance. This work was supported by funds from the Ministry of Science and Technology (grant no. 2009CB918801 to Y.S., and 2012CB910900 to X.W.D.), the National Natural Science

Foundation, and the Beijing Municipal Commissions of Education and Science and Technology. AUTHOR INFORMATION Author notes * Di Wu, Qi Hu and Zhen Yan: These authors contributed equally to

this work. AUTHORS AND AFFILIATIONS * Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing,

100084, China Di Wu, Qi Hu, Zhen Yan, Jing Zhang, Haiteng Deng & Yigong Shi * College of Life Sciences, Peking University, Beijing, 100871, China Wen Chen, Xi Huang, Panyu Yang & 

XingWang Deng * State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing,

100084, China Chuangye Yan & Jiawei Wang * Peking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, State Key Laboratory of Protein and Plant Gene Research, Peking

University, Beijing, 100871, China Xi Huang, Panyu Yang & XingWang Deng Authors * Di Wu View author publications You can also search for this author inPubMed Google Scholar * Qi Hu View

author publications You can also search for this author inPubMed Google Scholar * Zhen Yan View author publications You can also search for this author inPubMed Google Scholar * Wen Chen

View author publications You can also search for this author inPubMed Google Scholar * Chuangye Yan View author publications You can also search for this author inPubMed Google Scholar * Xi

Huang View author publications You can also search for this author inPubMed Google Scholar * Jing Zhang View author publications You can also search for this author inPubMed Google Scholar *

Panyu Yang View author publications You can also search for this author inPubMed Google Scholar * Haiteng Deng View author publications You can also search for this author inPubMed Google

Scholar * Jiawei Wang View author publications You can also search for this author inPubMed Google Scholar * XingWang Deng View author publications You can also search for this author

inPubMed Google Scholar * Yigong Shi View author publications You can also search for this author inPubMed Google Scholar CONTRIBUTIONS D.W., Q.H., H.D., X.W.D. and Y.S. designed all

experiments. D.W., Q.H., Z.Y., W.C., C.Y. and J.Z. performed the experiments. D.W., Q.H., Z.Y., W.C., C.Y., X.H., J.Z., P.Y., H.D., J.W., X.W.D. and Y.S. contributed to technical work and

data analysis. D.W., Q.H., Z.Y., W.C., C.Y., J.W., X.W.D. and Y.S. contributed to manuscript preparation. Y.S. wrote the manuscript. CORRESPONDING AUTHOR Correspondence to Yigong Shi. ETHICS

DECLARATIONS COMPETING INTERESTS The authors declare no competing financial interests. SUPPLEMENTARY INFORMATION SUPPLEMENTARY INFORMATION This file contains Supplementary Figures 1-14 with

legends, Supplementary Table 1 and additional references. (PDF 1491 kb) POWERPOINT SLIDES POWERPOINT SLIDE FOR FIG. 1 POWERPOINT SLIDE FOR FIG. 2 POWERPOINT SLIDE FOR FIG. 3 POWERPOINT

SLIDE FOR FIG. 4 RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Di Wu, Hu, Q., Yan, Z. _et al._ Structural basis of ultraviolet-B perception by UVR8.

_Nature_ 484, 214–219 (2012). https://doi.org/10.1038/nature10931 Download citation * Received: 17 November 2011 * Accepted: 10 February 2012 * Published: 29 February 2012 * Issue Date: 12

April 2012 * DOI: https://doi.org/10.1038/nature10931 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable

link is not currently available for this article. Copy to clipboard Provided by the Springer Nature SharedIt content-sharing initiative