{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vogeley L"],"funding":["NIGMS NIH HHS"],"pagination":["1390-3"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5017883"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["306(5700)"],"pubmed_abstract":["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."],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A."],"pmcid":["PMC5017883"],"funding_grant_id":["R01 GM067808","R01-GM067808","R37-GM27750","R01 GM059970","R01-GM59970","R37 GM027750"],"pubmed_authors":["Sasaki J","Sineshchekov OA","Trivedi VD","Spudich JL","Luecke H","Vogeley L"],"additional_accession":[]},"is_claimable":false,"name":"Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A.","description":"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.","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Nov","modification":"2020-11-19T16:07:07Z","creation":"2019-03-27T02:23:53Z"},"accession":"S-EPMC5017883","cross_references":{"pubmed":["15459346"],"doi":["10.1126/science.1103943"]}}