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Published Online September 30, 2004
Science DOI: 10.1126/science.1103943

Reports

Submitted on August 11, 2004
Accepted on September 22, 2004

Anabaena Sensory Rhodopsin: A Photochromic Color Sensor at 2.0 Å

Lutz Vogeley 1, Oleg A. Sineshchekov 2, Vishwa D. Trivedi 3, Jun Sasaki 3, John L. Spudich 4*, Hartmut Luecke 5*

1 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.
2 Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA; Biology Department, Moscow State University, Moscow, Russia.
3 Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA.
4 Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA; Department of Microbiology and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA.
5 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA; Department of Physiology and Biophysics and Department of Informatics and Computer Sciences, University of California, Irvine, CA 92697, USA.

* To whom correspondence should be addressed.
John L. Spudich , E-mail: john.l.spudich{at}uth.tmc.edu
Hartmut Luecke , E-mail: hudel{at}uci.edu

Microbial sensory rhodopsins are a family of membrane-embedded photoreceptors in prokaryotic and eukaryotic organisms. Structures of archaeal rhodopsins, which function as light-driven ion pumps or photosensors, have been reported. We present the structure of a eubacterial rhodopsin, which differs from those of previously characterized archaeal rhodopsins in its chromophore and cytoplasmic-side portions. Anabaena sensory rhodopsin exhibits light-induced interconversion between stable 13-cis and all-trans states of the retinylidene protein. The ratio of its cis and trans chromophore forms depends on the wavelength of illumination, thus providing a mechanism for how a single protein can signal the color of light, for example regulating color-sensitive processes such as differential photosynthetic light-harvesting pigment synthesis (chromatic adaptation). Its cytoplasmic half channel, highly hydrophobic in the archaeal rhodopsins, contains numerous hydrophilic residues networked by water molecules, providing a connection from the photoactive site to the cytoplasmic surface believed to interact with the receptor's soluble 14-kDa transducer.


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