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[[Image:1u3d.jpg|left|200px]]
[[Image:1u3d.jpg|left|200px]]


{{Structure
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|RELATEDENTRY=[[1u3c|1U3C]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3d OCA], [http://www.ebi.ac.uk/pdbsum/1u3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u3d RCSB]</span>
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'''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'''
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[[Category: Smith, B S.]]
[[Category: Smith, B S.]]
[[Category: Tomchick, D R.]]
[[Category: Tomchick, D R.]]
[[Category: amppnp]]
[[Category: Amppnp]]
[[Category: photolyase]]
[[Category: Photolyase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:42:44 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:51 2008''

Revision as of 07:42, 3 May 2008

File:1u3d.jpg

Template:STRUCTURE 1u3d

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


Overview

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

1U3D is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

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:15299148 Page seeded by OCA on Sat May 3 10:42:44 2008

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