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ReportsAnabaena Sensory Rhodopsin: A Photochromic Color Sensor at 2.0 Å
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 a single protein to signal the color of light, for example, to regulate color-sensitive processes such as chromatic adaptation in photosynthesis. 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-kilodalton transducer.
1 Department of Molecular Biology and Biochemistry,
2 Department of Physiology and Biophysics and Department of Informatics and Computer Sciences, University of California, Irvine, CA 92697, USA. 3 Center for Membrane Biology, Department of Biochemistry and Molecular Biology, 4 Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX 77030, USA. 5 Biology Department, Moscow State University, Moscow, Russia. * To whom correspondence should be addressed. E-mail: hudel{at}uci.edu (H.L.) or john.l.spudich{at}uth.tmc.edu (J.L.S.)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)