Conformational activation of visual rhodopsin in native disc membranes

• Rhodopsin is the G protein-coupled receptor (GPCR) that serves as a dim-light receptor for vision in vertebrates. We probed light-induced conformational changes in rhodopsin in its native membrane environment at room temperature using time-resolved wide-angle x-ray scattering. We observed a rapid conformational transition that is consistent with an outward tilt of the cytoplasmic portion of transmembrane helix 6 concomitant with an inward movement of the cytoplasmic portion of transmembrane helix 5. These movements were considerably larger than those reported from the basis of crystal structures of activated rhodopsin, implying that light activation of rhodopsin involves a more extended conformational change than was previously suggested.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine (hsv//eng)

Keyword

PROTEIN-COUPLED RECEPTOR

X-RAY-SCATTERING

PHOTOACTIVE YELLOW PROTEIN

TIME-RESOLVED WAXS

CRYSTAL-STRUCTURE

STRUCTURAL DYNAMICS

FLUORESCENCE

SPECTROSCOPY

METARHODOPSIN-II

BOVINE RHODOPSIN

BINDING-SITE

Biochemistry & Molecular Biology

Cell Biology

Publication and Content Type

ref (subject category)

art (subject category)