Research ArticleStructural Biology

Conformational activation of visual rhodopsin in native disc membranes

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Science Signaling  10 Mar 2015:
Vol. 8, Issue 367, pp. ra26
DOI: 10.1126/scisignal.2005646

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Lighting up rhodopsin movement

One of the fastest signaling events is the eye’s response to light, which is detected by rhodopsin, a member of the seven-transmembrane G protein [heterotrimeric guanine nucleotide–binding protein]–coupled receptors (GPCRs). Although many structural analyses have been done with this and other GPCRs, few have been performed with the proteins in their native membrane environment. Malmerberg et al. used time-resolved wide-angle x-ray scattering to identify light-induced conformational changes in rhodopsin in its native membrane at room temperature. Within a few milliseconds, rhodopsin adopted a stable active conformation that was associated with a large movement of portions of two adjacent transmembrane domains.