Sensory rhodopsin II: functional insights from structure.
Atomic resolution structures of a sensory rhodopsin phototaxis receptor in haloarchaea (the first sensory member of the widespread microbial rhodopsin family) have yielded insights into the interaction face with its membrane-embedded transducer and into the mechanism of spectral tuning. Spectral differences between sensory rhodopsin and the light-driven proton pump bacteriorhodopsin depend largely upon the repositioning of a conserved arginine residue in the chromophore-binding pocket. Information derived from the structures, combined with biophysical and biochemical analysis, has established a model for receptor activation and signal relay, in which light-induced helix tilting in the receptor is transmitted to the transducer by lateral transmembrane helix-helix interactions.
Spudich
John L
JL
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77030, USA. John.L.Spudich@uth.tmc.edu
Luecke
Hartmut
H
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000528:radiation effects; D002338:Carotenoids / Q000737:chemistry* / Q000378:metabolism* / Q000528:radiation effects; D002462:Cell Membrane / Q000737:chemistry; D018360:Crystallography, X-Ray; D025602:Halorhodopsins; D008027:Light; D008958:Models, Molecular; D019633:Natronobacterium / Q000737:chemistry* / Q000378:metabolism / Q000528:radiation effects; D010777:Photochemistry; D011487:Protein Conformation; D025603:Sensory Rhodopsins; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship
D019843:Archaeal Proteins; D025602:Halorhodopsins; C434451:HtrII protein, Natronobacterium pharaonis; D025603:Sensory Rhodopsins; C434450:phototaxis receptor sensory rhodopsin II, Natronobacterium pharaonis; C061508:sensory rhodopsin II protein, archaeal; D002338:Carotenoids