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Science. 2007 May 18;316(5827):1054-7.

Conformational switching in the fungal light sensor Vivid.

Author information

1
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.

Abstract

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).

PMID:
17510367
PMCID:
PMC3682417
DOI:
10.1126/science.1137128
[Indexed for MEDLINE]
Free PMC Article

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