View source for 4dnu


==Crystal structure of the W285A mutant of UVB-resistance protein UVR8==
<StructureSection load='4dnu' size='340' side='right' caption='[[4dnu]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dnu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DNU FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dnv|4dnv]], [[4dnw|4dnw]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UVR8, At5g63860, AT5G63860 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dnu OCA], [http://pdbe.org/4dnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dnu RCSB], [http://www.ebi.ac.uk/pdbsum/4dnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dnu ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/UVR8_ARATH UVR8_ARATH]] UV-B specific signaling component that acts as UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV-B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore.<ref>PMID:16330762</ref> <ref>PMID:17720867</ref> <ref>PMID:18055587</ref> <ref>PMID:19165148</ref> <ref>PMID:19402876</ref> <ref>PMID:21041653</ref> <ref>PMID:21395889</ref> <ref>PMID:21454788</ref> <ref>PMID:22447155</ref> <ref>PMID:23161229</ref> <ref>PMID:23012433</ref> <ref>PMID:22988111</ref>  
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== Publication Abstract from PubMed ==
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 A resolution, revealing a symmetric homodimer of seven-bladed beta-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-pi 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-pi interactions, causing disruption of the critical intermolecular hydrogen bonds mediated by Arg 286 and Arg 338 and subsequent dissociation of the UVR8 homodimer.

Structural basis of ultraviolet-B perception by UVR8.,Wu D, Hu Q, Yan Z, Chen W, Yan C, Huang X, Zhang J, Yang P, Deng H, Wang J, Deng X, Shi Y Nature. 2012 Feb 29;484(7393):214-9. doi: 10.1038/nature10931. PMID:22388820<ref>PMID:22388820</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4dnu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Suggestions for new articles|Suggestions for new articles]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Chen, W]]
[[Category: Hu, Q]]
[[Category: Shi, Y]]
[[Category: Wang, J]]
[[Category: Wu, D]]
[[Category: Yan, C]]
[[Category: Yan, Z]]
[[Category: Zhang, J]]
[[Category: Cop1]]
[[Category: Gene regulation]]
[[Category: Uv-b perception]]
[[Category: Wd40 repeat]]