Sensory rhodopsin II: functional insights from structure
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Published on: October 4, 2024
John L Spudich1, Hartmut Luecke
1Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77030, USA. John.L.Spudich@uth.tmc.edu
Abstract:
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.
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