Arrangement of rhodopsin transmembrane α-helices

Vinzenz M. Unger, Paul A. Hargrave, Joyce M. Baldwin and Gebhard F. X. Schertler ()
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Vinzenz M. Unger: MRC Laboratory of Molecular Biology
Paul A. Hargrave: Department of Ophthalmology
Joyce M. Baldwin: MRC Laboratory of Molecular Biology
Gebhard F. X. Schertler: MRC Laboratory of Molecular Biology

Nature, 1997, vol. 389, issue 6647, 203-206

Abstract: Abstract Rhodopsins1, the photoreceptors in rod cells, are G-protein-coupled receptors with seven hydrophobic segments containing characteristic conserved sequence patterns that define a large family2,3. Members of the family are expected to share a conserved transmembrane structure. Direct evidence for the arrangement of seven α-helices was obtained from a 9å projection map of bovine rhodopsin4. Structural constraints inferred from a comparison of G-protein-coupled receptor sequences were used to assign the seven hydrophobic stretches in the sequence to features in the projection map5. A low-resolution three-dimensional structure of bovine rhodopsin6 and two projection structures of frog rhodopsin7 confirmed the position of the three least tilted helices, 4, 6 and 7. A more elongated peak of density for helix 5 indicated that it is tilted or bent6,7, but helices 1, 2 and 3 were not resolved. Here we have used electron micrographs of frozen-hydrated two-dimensional frog rhodopsin crystals to determine the structure of frog rhodopsin. Seven rods of density in the map are used to estimate tilt angles for the seven helices. Density visible on the extracellular side of the membrane suggests a folded domain. Density extends from helix 6 on the intracellular side, and a short connection between helices 1 and 2, and possibly a part of the carboxy terminus, are visible.

Date: 1997
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DOI: 10.1038/38316

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