Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana

Chad A Brautigam, Barbara S. Smith, Zhiquan Ma, Maya Palnitkar, Diana R Tomchick, Mischa Machius, Johann Deisenhofer

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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.

Original languageEnglish (US)
Pages (from-to)12142-12147
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number33
DOIs
StatePublished - Aug 17 2004

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