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Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin
TLDR
Disulfide cross-linking of the helices prevented activation of transducin, which suggests the importance of this movement for activation of rhodopsin.
Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S
TLDR
The toxic constitutively active rhodopsin mutant, E113Q/E134Q/M257Y, previously shown to require inducible expression, has now been expressed in an HEK293S GNTI−-inducible cell line at levels comparable with those obtained with WT rhodopin.
Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.
TLDR
It is concluded that glutamic acid-113 serves as the retinylidene Schiff base counterion in rhodopsin and this opsin-chromophore interaction is an example of a general mechanism of color regulation in the visual pigments.
A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin.
TLDR
Ten mutants of bacteriorhodopsin, each containing a single cysteine residue regularly spaced along helix D and facing the lipid bilayer, were derivatized with a nitroxide spin label to provide a general strategy for determining the immersion depth of nitroxides in bilayers.
Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants.
TLDR
The application to one polypeptide segment in bacteriorhodopsin, a transmembrane chromoprotein that functions as a light-driven proton pump, indicates that residues 129 to 131 form a short water-exposed loop, while residues 132 to 142 are membrane-embedded.
Identification of core amino acids stabilizing rhodopsin.
TLDR
Rhodopsin is the only G protein-coupled receptor whose 3D structure is known; therefore, it serves as a prototype for studies of the GPCR family of proteins and its core includes the C110-C187 disulfide bond.
Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin.
TLDR
Of the 10 cysteines in bovine rhodopsin, only intradiscal Cys-110 and Cys -187 are essential for the correct tertiary structure of the protein.
Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212.
TLDR
A model for the proton-pumping mechanism of bR is derived, which features proton transfers among Asp-85, -96, and -212, the chromophore Schiff base, and other ionizable groups within the protein.
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