Structural basis for the photoconversion of a phytochrome to the activated Pfr form
Andrew T. Ulijasz,
Gabriel Cornilescu,
Claudia C. Cornilescu,
Junrui Zhang,
Mario Rivera,
John L. Markley and
Richard D. Vierstra ()
Additional contact information
Andrew T. Ulijasz: Department of Genetics and,
Gabriel Cornilescu: National Magnetic Resonance Facility at Madison, University of Wisconsin–Madison, Madison, Wisconsin 53706, USA
Claudia C. Cornilescu: National Magnetic Resonance Facility at Madison, University of Wisconsin–Madison, Madison, Wisconsin 53706, USA
Junrui Zhang: Department of Genetics and,
Mario Rivera: Multidisciplinary Research Building, University of Kansas, Lawrence, Kansas 66057-1620, USA
John L. Markley: National Magnetic Resonance Facility at Madison, University of Wisconsin–Madison, Madison, Wisconsin 53706, USA
Richard D. Vierstra: Department of Genetics and,
Nature, 2010, vol. 463, issue 7278, 250-254
Abstract:
Photoactivated phytochromes Phytochromes are a family of bilin-containing photoreceptors that regulate various processes in plants and microorganisms. These photoreceptors interconvert between a red-light-absorbing ground state (Pr) and a far-red-light-absorbing photoactivated state (Pfr). The structures of the Pr state of several phytochromes have been determined, but little is known about the Pfr state. In this paper, the authors determined that light-induced rotation of the A ring of the bilin is the primary motion of the chromophore during photoconversion. Subsequent rearrangements within the protein then affect intra- and interdomain contact sites within the phytochrome dimer.
Date: 2010
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DOI: 10.1038/nature08671
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