1U3C

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

Summary for 1U3C

• Entry DOI: 10.2210/pdb1u3c/pdb
• Related: 1u3d
• Descriptor: Cryptochrome 1 apoprotein, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: photolyase, amppnp, signaling protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Cytoplasm: Q43125
• Total number of polymer chains: 1
• Total formula weight: 58807.25

Authors

Brautigam, C.A.,Smith, B.S.,Ma, Z.,Palnitkar, M.,Tomchick, D.R.,Machius, M.,Deisenhofer, J. (deposition date: 2004-07-21, release date: 2004-08-24, Last modification date: 2024-11-20)

Primary citation

Brautigam, C.A.,Smith, B.S.,Ma, Z.,Palnitkar, M.,Tomchick, D.R.,Machius, M.,Deisenhofer, J.
Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana.
Proc.Natl.Acad.Sci.USA, 101:12142-12147, 2004

PubMed Abstract: 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.

PubMed: 15299148
DOI: 10.1073/pnas.0404851101

Experimental method

X-RAY DIFFRACTION (2.6 Å)