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Structural basis for the photoconversion of a phytochrome to the activated far-red light-absorbing form
dc.contributor.author | Ulijasz, Andrew T. | |
dc.contributor.author | Cornilescu, Gabriel | |
dc.contributor.author | Cornilescu, Claudia C. | |
dc.contributor.author | Zhang, Junrui | |
dc.contributor.author | Rivera, Mario | |
dc.contributor.author | Markley, John L. | |
dc.contributor.author | Vierstra, Richard D. | |
dc.date.accessioned | 2017-04-27T16:49:06Z | |
dc.date.available | 2017-04-27T16:49:06Z | |
dc.date.issued | 2010-01-14 | |
dc.identifier.citation | Ulijasz, A. T., Cornilescu, G., Cornilescu, C. C., Zhang, J., Rivera, M., Markley, J. L., & Vierstra, R. D. (2010). STRUCTURAL BASIS FOR THE PHOTOCONVERSION OF A PHYTOCHROME TO THE ACTIVATED FAR-RED LIGHT-ABSORBING FORM. Nature, 463(7278), 250–254. http://doi.org/10.1038/nature08671 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/23834 | |
dc.description.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 Pfr1,2. While the structures of several phytochromes as Pr have been determined3-7, little is known about the structure of Pfr and how it initiates signaling. 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 but not the D pyrrole ring 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. From 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. | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.title | Structural basis for the photoconversion of a phytochrome to the activated far-red light-absorbing form | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Rivera, Mario | |
kusw.kudepartment | Chemistry | en_US |
dc.identifier.doi | 10.1038/nature08671 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC2807988 | en_US |
dc.rights.accessrights | openAccess |