Sensory rhodopsin II: functional insights from structure.

John L Spudich, Hartmut Luecke

Journal: Current opinion in structural biology 2003;12(4):540-6

PMID: 12163079

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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.

Address: Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77030, USA. [email protected]

DOI: 10.1016/s0959-440x(02)00359-7

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MeSH Terms: Archaeal Proteins, Carotenoids, Cell Membrane, Crystallography, X-Ray, Halorhodopsins, Light, Models, Molecular, Natronobacterium, Photochemistry, Protein Conformation, Sensory Rhodopsins, Signal Transduction, Structure-Activity Relationship