1u3c: Difference between revisions

Revision as of 05:22, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1u3c.png

Template:STRUCTURE 1u3c

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

Template:ABSTRACT PUBMED 15299148

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

Page seeded by OCA on Tue Jul 29 05:22:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana'''
+===Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299148}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299148 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15299148}}
 ==About this Structure==
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 [[Category: Amppnp]]
 [[Category: Photolyase]]
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