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1u3c

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(New page: 200px<br /><applet load="1u3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u3c, resolution 2.60&Aring;" /> '''Crystal Structure of...)
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Revision as of 01:41, 21 November 2007

Image:1u3c.jpg

1u3c, resolution 2.60Å

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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.

About this Structure

1U3C is a Single protein structure of sequence from Arabidopsis thaliana with MG, CL, FAD, NDS and HEZ as ligands. 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

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