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J. Biol. Chem., Vol. 279, Issue 25, 26417-26424, June 18, 2004

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Initial Events in the Photocycle of Photoactive Yellow Protein^*

Remco Kort¶||, Klaas J. Hellingwerf, and Raimond B. G. Ravelli¶**

From the Laboratory for Microbiology, Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands, the European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble Cedex, France, and the ^**European Molecular Biology Laboratory Grenoble Outstation, B.P. 181, F-38042 Grenoble Cedex 9, France

The light-induced isomerization of a double bond is the key event that allows the conversion of light energy into a structural change in photoactive proteins for many light-mediated biological processes, such as vision, photosynthesis, photomorphogenesis, and photo movement. Cofactors such as retinals, linear tetrapyrroles, and 4-hydroxy-cinnamic acid have been selected by nature that provide the essential double bond to transduce the light signal into a conformational change and eventually, a physiological response. Here we report the first events after light excitation of the latter chromophore, containing a single ethylene double bond, in a low temperature crystallographic study of the photoactive yellow protein. We measured experimental phases to overcome possible model bias, corrected for minimized radiation damage, and measured absorption spectra of crystals to analyze the photoproducts formed. The data show a mechanism for the light activation of photoactive yellow protein, where the energy to drive the remainder of the conformational changes is stored in a slightly strained but fully cis-chromophore configuration. In addition, our data indicate a role for backbone rearrangements during the very early structural events.

Received for publication, October 31, 2003 , and in revised form, March 8, 2004.

The atomic coordinates and structure factors (codes 1UWN and 1UWP) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ These authors contributed equally to this work.

^|| To whom correspondence should be addressed. Tel.: 31205257062; Fax: 31205257056; E-mail: rkort{at}science.uva.nl.

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