1u3c: Difference between revisions
New page: left|200px<br /><applet load="1u3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u3c, resolution 2.60Å" /> '''Crystal Structure of... |
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[[Image:1u3c.jpg|left|200px]]<br /><applet load="1u3c" size=" | [[Image:1u3c.jpg|left|200px]]<br /><applet load="1u3c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1u3c, resolution 2.60Å" /> | caption="1u3c, resolution 2.60Å" /> | ||
'''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana'''<br /> | '''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana'''<br /> | ||
==Overview== | ==Overview== | ||
Signals generated by cryptochrome (CRY) blue-light photoreceptors are | 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== | ==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 MG, CL, FAD, NDS and HEZ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brautigam, C | [[Category: Brautigam, C A.]] | ||
[[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 | [[Category: Smith, B S.]] | ||
[[Category: Tomchick, D | [[Category: Tomchick, D R.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: photolyase]] | [[Category: photolyase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:17 2008'' | ||
Revision as of 16:20, 21 February 2008
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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 with , , , and as ligands. 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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