1u3c: Difference between revisions

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[[Image:1u3c.jpg|left|200px]]<br /><applet load="1u3c" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1u3c.jpg|left|200px]]
caption="1u3c, resolution 2.60&Aring;" />
 
'''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana'''<br />
{{Structure
|PDB= 1u3c |SIZE=350|CAPTION= <scene name='initialview01'>1u3c</scene>, resolution 2.60&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NDS:ETHYL+DIMETHYL+AMMONIO+PROPANE+SULFONATE'>NDS</scene> and <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>
|ACTIVITY=
|GENE= CRY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
}}
 
'''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1U3C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=NDS:'>NDS</scene> and <scene name='pdbligand=HEZ:'>HEZ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U3C OCA].  
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].  


==Reference==
==Reference==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299148 15299148]
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]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: photolyase]]
[[Category: photolyase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:17 2008''
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Revision as of 15:26, 20 March 2008

File:1u3c.jpg


PDB ID 1u3c

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands: , , , and
Gene: CRY1 (Arabidopsis thaliana)
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 StructureAbout this Structure

1U3C is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

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

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