-
- Oleg A. Sineshchekov
- Department of Molecular Biology and Biochemistry,
-
- Lutz Vogeley
- Department of Molecular Biology and Biochemistry,
-
- Vishwa D. Trivedi
- Department of Molecular Biology and Biochemistry,
-
- Hartmut Luecke
- Department of Molecular Biology and Biochemistry,
-
- John L. Spudich
- Department of Molecular Biology and Biochemistry,
-
- Jun Sasaki
- Department of Molecular Biology and Biochemistry,
書誌事項
- 公開日
- 2004-11-19
- DOI
-
- 10.1126/science.1103943
- 公開者
- American Association for the Advancement of Science (AAAS)
この論文をさがす
説明
<jats:p> 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. <jats:italic>Anabaena</jats:italic> 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. </jats:p>
収録刊行物
-
- Science
-
Science 306 (5700), 1390-1393, 2004-11-19
American Association for the Advancement of Science (AAAS)
