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


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.

SUBMITTER: Brautigam CA 

PROVIDER: S-EPMC514401 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature

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

Brautigam Chad A CA   Smith Barbara S BS   Ma Zhiquan Z   Palnitkar Maya M   Tomchick Diana R DR   Machius Mischa M   Deisenhofer Johann J  

Proceedings of the National Academy of Sciences of the United States of America 20040806 33


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  ...[more]

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