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First published online April 29, 2002; 10.1105/tpc.010475

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The Plant Cell, Vol. 14, 1067-1075, May 2002, Copyright © 2002,
American Society of Plant Biologists

Photoexcited Structure of a Plant Photoreceptor Domain Reveals a Light-Driven Molecular Switch

Sean Crossona and Keith Moffat1,a,b,c

a Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637
b Consortium for Advanced Radiation Sources, University of Chicago, Chicago, Illinois 60637
c Institute for Biophysical Dynamics, University of Chicago, Chicago, Illinois 60637

1 To whom correspondence should be addressed. E-mail moffat{at}cars.uchicago.edu; fax 773-702-0439

The phototropins are flavoprotein kinases that control phototropic bending, light-induced chloroplast movement, and stomatal opening in plants. Two flavin mononucleotide binding light, oxygen, or voltage (LOV) domains are the sites for initial photochemistry in these blue light photoreceptors. We have determined the steady state, photoexcited crystal structure of a flavin-bound LOV domain. The structure reveals a unique photochemical switch in the flavin binding pocket in which the absorption of light drives the formation of a reversible covalent bond between a highly conserved Cys residue and the flavin cofactor. This provides a molecular picture of a cysteinyl-flavin covalent adduct, the presumed signaling species that leads to phototropin kinase activation and subsequent signal transduction. We identify closely related LOV domains in two eubacterial proteins that suggests the light-induced conformational change evident in this structure is an ancient biomolecular response to light, arising before the appearance of plants.




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