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Crystal structure of squid rhodopsin

Naturevolume 453, pages363–367 (2008)Cite this article

Abstract

Invertebrate phototransduction uses an inositol-1,4,5-trisphosphate signalling cascade in which photoactivated rhodopsin stimulates a Gq-type G protein, that is, a class of G protein that stimulates membrane-bound phospholipase Cβ. The same cascade is used by many G-protein-coupled receptors, indicating that invertebrate rhodopsin is a prototypical member. Here we report the crystal structure of squid (Todarodes pacificus) rhodopsin at 2.5 Å resolution. Among seven transmembrane α-helices, helices V and VI extend into the cytoplasmic medium and, together with two cytoplasmic helices, they form a rigid protrusion from the membrane surface. This peculiar structure, which is not seen in bovine rhodopsin, seems to be crucial for the recognition of Gq-type G proteins. The retinal Schiff base forms a hydrogen bond to Asn 87 or Tyr 111; it is far from the putative counterion Glu 180. In the crystal, a tight association is formed between the amino-terminal polypeptides of neighbouring monomers; this intermembrane dimerization may be responsible for the organization of hexagonally packed microvillar membranes in the photoreceptor rhabdom.

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Figure 1:Schematic diagram of the topology of squid rhodopsin.
Figure 2:Crystal structure of C-terminally truncated squid rhodopsin.
Figure 3:Structural comparisons between squid rhodopsin and bovine rhodopsin.
Figure 4:Retinal-binding pocket and interhelical cavity.
Figure 5:Cytoplasmic view of C-terminally truncated squid rhodopsin.

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Accession codes

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Protein Data Bank

Data deposits

The coordinates have been deposited in the Protein Data Bank under accession number2z73.

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Acknowledgements

This work was supported by Grant-in-Aids from the Ministry of Education, Science and Culture of Japan and partly by the National Project on Protein Structural and Functional Analyses.

Author Contributions T.K. and M.M. designed the project. M.M. performed all experiments. T.K. assisted in data collection and structure determination. T.K. and M.M. jointly wrote the manuscript.

Author information

Authors and Affiliations

  1. Department of Physics, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan

    Midori Murakami & Tsutomu Kouyama

  2. RIKEN Harima Institute/SPring-8, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan,

    Tsutomu Kouyama

Authors
  1. Midori Murakami
  2. Tsutomu Kouyama

Corresponding author

Correspondence toTsutomu Kouyama.

Supplementary information

Supplementary information

The file contains Supplementary Tables S1-S2, Figure S1 and Legends. Supplementary Table S1 includes X-ray data collection and refinement statistics. Supplementary Table S2 shows the distances to the closest atoms of all amino acids around the retinal. Supplementary Figure S1 shows the multiple sequence alignment of squid and bovine rhodopsins. (PDF 371 kb)

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Editorial Summary

Squid rhodopsin: A structure for signal transduction

The rhodopsins found in the invertebrate eye are light-activated G-protein-coupled receptors, whose activity is coupled to Gq-type G-proteins. Midori Murakami and Tsutomu Kouyama now report the crystal structure of squid rhodopsin, at 2.5 Å, in which a putative G-protein-binding site is resolved. The newly obtained structure could help explain one of the novel properties of the invertebrate eye, the ability to detect the direction of the polarization plane of visible light.

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