Photoreceptor proteins, "star actors of modern times": a review of the functional dynamics in the structure of representative members of six different photoreceptor families.
Six well-characterized photoreceptor families function in Nature to mediate light-induced signal transduction: the rhodopsins, phytochromes, xanthopsins, cryptochromes, phototropins, and BLUF proteins. The first three catalyze E/Z isomerization of retinal, phytochromobilin, and p-coumaric acid, respectively, while the last three all have a different flavin-based photochemistry. For many of these photoreceptor proteins, (many of) the details of the conversion of the light-induced change in configuration of their chromophore into a signaling state and eventually a biological response have been resolved. Some members of the rhodopsins, the xanthopsins, and the phototropins are so well characterized that they function as model systems to study (receptor) protein dynamics and (un)folding.
van der Horst
Michael A
MA
Laboratory for Microbiology, Swammerdam Institute for Life Sciences, BioCentrum Amsterdam, University of Amsterdam, NL-1018 WV Amsterdam, The Netherlands.
Hellingwerf
Klaas J
KJ
D000818:Animals; D056931:Cryptochromes; D029721:Drosophila Proteins; D005136:Eye Proteins; D005420:Flavoproteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D015394:Molecular Structure; D017956:Photoreceptor Cells, Invertebrate; D020283:Photoreceptors, Microbial / Q000737:chemistry / Q000502:physiology*; D010834:Phytochrome / Q000737:chemistry / Q000502:physiology*; D011487:Protein Conformation; D043562:Receptors, G-Protein-Coupled; D012243:Rhodopsin / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology
D056931:Cryptochromes; D029721:Drosophila Proteins; D005136:Eye Proteins; D005420:Flavoproteins; D020283:Photoreceptors, Microbial; D043562:Receptors, G-Protein-Coupled; C119828:cry protein, Drosophila; D010834:Phytochrome; D012243:Rhodopsin