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==Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana== | |||
<StructureSection load='1u3c' size='340' side='right'caption='[[1u3c]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1u3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U3C FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDS:ETHYL+DIMETHYL+AMMONIO+PROPANE+SULFONATE'>NDS</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3c OCA], [https://pdbe.org/1u3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u3c RCSB], [https://www.ebi.ac.uk/pdbsum/1u3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u3c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CRY1_ARATH CRY1_ARATH] Mediates blue light-induced gene expression through the inhibition of COP1-mediated degradation of the transcription factor BIT1. Involved in blue light-dependent stomatal opening, CHS gene expression, inhibition of stem growth and increase of root growth.<ref>PMID:7756321</ref> <ref>PMID:9565033</ref> <ref>PMID:16093319</ref> <ref>PMID:16703358</ref> <ref>PMID:18397371</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u3/1u3c_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u3c ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Signals generated by cryptochrome (CRY) blue-light photoreceptors are responsible for a variety of developmental and circadian responses in plants. The CRYs are also identified as circadian blue-light photoreceptors in Drosophila and components of the mammalian circadian clock. These flavoproteins all have an N-terminal domain that is similar to photolyase, and most have an additional C-terminal domain of variable length. We present here the crystal structure of the photolyase-like domain of CRY-1 from Arabidopsis thaliana. The structure reveals a fold that is very similar to photolyase, with a single molecule of FAD noncovalently bound to the protein. The surface features of the protein and the dissimilarity of a surface cavity to that of photolyase account for its lack of DNA-repair activity. Previous in vitro experiments established that the photolyase-like domain of CRY-1 can bind Mg.ATP, and we observe a single molecule of an ATP analog bound in the aforementioned surface cavity, near the bound FAD cofactor. The structure has implications for the signaling mechanism of CRY blue-light photoreceptors. | |||
Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana.,Brautigam CA, Smith BS, Ma Z, Palnitkar M, Tomchick DR, Machius M, Deisenhofer J Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12142-7. Epub 2004 Aug 6. PMID:15299148<ref>PMID:15299148</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1u3c" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Cryptochrome 3D structures|Cryptochrome 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Brautigam | [[Category: Large Structures]] | ||
[[Category: Deisenhofer | [[Category: Brautigam CA]] | ||
[[Category: Ma | [[Category: Deisenhofer J]] | ||
[[Category: Machius | [[Category: Ma Z]] | ||
[[Category: Palnitkar | [[Category: Machius M]] | ||
[[Category: Smith | [[Category: Palnitkar M]] | ||
[[Category: Tomchick | [[Category: Smith BS]] | ||
[[Category: Tomchick DR]] | |||
Latest revision as of 03:32, 21 November 2024
Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thalianaCrystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana
Structural highlights
FunctionCRY1_ARATH Mediates blue light-induced gene expression through the inhibition of COP1-mediated degradation of the transcription factor BIT1. Involved in blue light-dependent stomatal opening, CHS gene expression, inhibition of stem growth and increase of root growth.[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSignals generated by cryptochrome (CRY) blue-light photoreceptors are responsible for a variety of developmental and circadian responses in plants. The CRYs are also identified as circadian blue-light photoreceptors in Drosophila and components of the mammalian circadian clock. These flavoproteins all have an N-terminal domain that is similar to photolyase, and most have an additional C-terminal domain of variable length. We present here the crystal structure of the photolyase-like domain of CRY-1 from Arabidopsis thaliana. The structure reveals a fold that is very similar to photolyase, with a single molecule of FAD noncovalently bound to the protein. The surface features of the protein and the dissimilarity of a surface cavity to that of photolyase account for its lack of DNA-repair activity. Previous in vitro experiments established that the photolyase-like domain of CRY-1 can bind Mg.ATP, and we observe a single molecule of an ATP analog bound in the aforementioned surface cavity, near the bound FAD cofactor. The structure has implications for the signaling mechanism of CRY blue-light photoreceptors. Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana.,Brautigam CA, Smith BS, Ma Z, Palnitkar M, Tomchick DR, Machius M, Deisenhofer J Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12142-7. Epub 2004 Aug 6. PMID:15299148[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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