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1u3c

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[[Image:1u3c.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana==
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|PDB= 1u3c |SIZE=350|CAPTION= <scene name='initialview01'>1u3c</scene>, resolution 2.60&Aring;
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<StructureSection load='1u3c' size='340' side='right'caption='[[1u3c]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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|GENE= CRY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[1u3d|1U3D]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3c OCA], [http://www.ebi.ac.uk/pdbsum/1u3c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u3c RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u3/1u3c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1u3c" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Cryptochrome 3D structures|Cryptochrome 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1U3C 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=1U3C OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brautigam, C A.]]
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[[Category: Brautigam CA]]
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[[Category: Deisenhofer, J.]]
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[[Category: Deisenhofer J]]
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[[Category: Ma, Z.]]
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[[Category: Ma Z]]
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[[Category: Machius, M.]]
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[[Category: Machius M]]
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[[Category: Palnitkar, M.]]
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[[Category: Palnitkar M]]
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[[Category: Smith, B S.]]
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[[Category: Smith BS]]
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[[Category: Tomchick, D R.]]
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[[Category: Tomchick DR]]
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[[Category: amppnp]]
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[[Category: photolyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:56 2008''
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Current revision

Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana

PDB ID 1u3c

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