期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 12, 期 4, 页码 540-546出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/S0959-440X(02)00359-7
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资金
- NIGMS NIH HHS [R01-GM56445, R01-GM27750] Funding Source: Medline
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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