Structure of full-length Drosophila cryptochrome

Brian D. Zoltowski, Anand T. Vaidya, Deniz Top, Joanne Widom, Michael W. Young and Brian R. Crane ()
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Brian D. Zoltowski: Cornell University
Anand T. Vaidya: Cornell University
Deniz Top: Laboratory of Genetics, The Rockefeller University
Joanne Widom: Cornell University
Michael W. Young: Laboratory of Genetics, The Rockefeller University
Brian R. Crane: Cornell University

Nature, 2011, vol. 480, issue 7377, 396-399

Abstract: Structure of a circadian photoreceptor The cryptochrome/photolyase family of photoreceptors mediates cellular responses to ultraviolet and blue light exposure in all kingdoms of life: cryptochromes transduce signals important for growth, development, magnetosensitivity and circadian clocks, and photolyases repair photolesions in DNA. Zoltowski et al. have now solved the X-ray crystal structure of full-length cryptochrome from Drosophila. They find that a C-terminal helix docks in a groove that is known to bind DNA substrates in photolyases, and a conserved tryptophan protrudes into the catalytic centre of the cryptochrome, mimicking how DNA-repair photolyases recognize lesions in DNA.

Date: 2011
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DOI: 10.1038/nature10618

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