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Science 18 May 2007:
Vol. 316. no. 5827, pp. 1054 - 1057
DOI: 10.1126/science.1137128
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Reports

Conformational Switching in the Fungal Light Sensor Vivid

Brian D. Zoltowski,1 Carsten Schwerdtfeger,2 Joanne Widom,1 Jennifer J. Loros,2,3 Alexandrine M. Bilwes,1 Jay C. Dunlap,2 Brian R. Crane1*

The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).

1 Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
2 Department of Genetics, Dartmouth Medical School, Hanover, NH 03755, USA.
3 Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.

* To whom correspondence should be addressed. E-mail: bc69{at}cornell.edu

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