4dnu: Difference between revisions
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==Crystal structure of the W285A mutant of UVB-resistance protein UVR8== | |||
<StructureSection load='4dnu' size='340' side='right' caption='[[4dnu]], [[Resolution|resolution]] 1.76Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4dnu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 Arabidopsis thaliana])</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://www.rcsb.org/pdb/explore.do?structureId=4dnu RCSB], [http://www.ebi.ac.uk/pdbsum/4dnu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Suggestions for new articles|Suggestions for new articles]] | *[[Suggestions for new articles|Suggestions for new articles]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Chen, W | [[Category: Chen, W]] | ||
[[Category: Hu, Q | [[Category: Hu, Q]] | ||
[[Category: Shi, Y | [[Category: Shi, Y]] | ||
[[Category: Wang, J | [[Category: Wang, J]] | ||
[[Category: Wu, D | [[Category: Wu, D]] | ||
[[Category: Yan, C | [[Category: Yan, C]] | ||
[[Category: Yan, Z | [[Category: Yan, Z]] | ||
[[Category: Zhang, J | [[Category: Zhang, J]] | ||
[[Category: Cop1]] | [[Category: Cop1]] | ||
[[Category: Gene regulation]] | [[Category: Gene regulation]] | ||
[[Category: Uv-b perception]] | [[Category: Uv-b perception]] | ||
[[Category: Wd40 repeat]] | [[Category: Wd40 repeat]] | ||
Revision as of 12:42, 21 December 2014
Crystal structure of the W285A mutant of UVB-resistance protein UVR8Crystal structure of the W285A mutant of UVB-resistance protein UVR8
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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