1u3c
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 MG, CL, FAD, NDS and HEZ 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
Page seeded by OCA on Wed Nov 21 03:49:09 2007