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Nature. 2010 Jan 14;463(7278):250-4. doi: 10.1038/nature08671.

Structural basis for the photoconversion of a phytochrome to the activated Pfr form.

Author information

1
Department of Genetics and, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Abstract

Phytochromes are a collection of bilin-containing photoreceptors that regulate numerous photoresponses in plants and microorganisms through their ability to photointerconvert between a red-light-absorbing, ground state (Pr) and a far-red-light-absorbing, photoactivated state (Pfr). Although the structures of several phytochromes as Pr have been determined, little is known about the structure of Pfr and how it initiates signalling. Here we describe the three-dimensional solution structure of the bilin-binding domain as Pfr, using the cyanobacterial phytochrome from Synechococcus OSB'. Contrary to predictions, light-induced rotation of the A pyrrole ring but not the D ring is the primary motion of the chromophore during photoconversion. Subsequent rearrangements within the protein then affect intradomain and interdomain contact sites within the phytochrome dimer. On the basis of our models, we propose that phytochromes act by propagating reversible light-driven conformational changes in the bilin to altered contacts between the adjacent output domains, which in most phytochromes direct differential phosphotransfer.

PMID:
20075921
PMCID:
PMC2807988
DOI:
10.1038/nature08671
[Indexed for MEDLINE]
Free PMC Article

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