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[[Image:1u3d.jpg|left|200px]]
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{{STRUCTURE_1u3d|  PDB=1u3d  |  SCENE=  }}
'''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana with AMPPNP bound'''


==Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana with AMPPNP bound==
<StructureSection load='1u3d' size='340' side='right'caption='[[1u3d]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1u3d]] 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=1U3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U3D 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]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=1u3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3d OCA], [https://pdbe.org/1u3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u3d RCSB], [https://www.ebi.ac.uk/pdbsum/1u3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u3d 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/u3/1u3d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1u3d 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1U3D is a [[Single protein]] structure of 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=1U3D OCA].
</div>
<div class="pdbe-citations 1u3d" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15299148 15299148]
*[[Cryptochrome 3D structures|Cryptochrome 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brautigam, C A.]]
[[Category: Brautigam CA]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer J]]
[[Category: Ma, Z.]]
[[Category: Ma Z]]
[[Category: Machius, M.]]
[[Category: Machius M]]
[[Category: Palnitkar, M.]]
[[Category: Palnitkar M]]
[[Category: Smith, B S.]]
[[Category: Smith BS]]
[[Category: Tomchick, D R.]]
[[Category: Tomchick DR]]
[[Category: Amppnp]]
[[Category: Photolyase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:42:44 2008''

Latest revision as of 06:37, 23 August 2023

Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana with AMPPNP bound

1u3d, resolution 2.45Å

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