2Z73
Crystal structure of squid rhodopsin
Summary for 2Z73
Entry DOI | 10.2210/pdb2z73/pdb |
Descriptor | Rhodopsin, octyl beta-D-glucopyranoside, RETINAL, ... (8 entities in total) |
Functional Keywords | visual pigment, gq-type, g-protein coupled receptor, chromophore, glycoprotein, lipoprotein, membrane, palmitate, phosphorylation, photoreceptor protein, retinal protein, sensory transduction, transducer, transmembrane, vision, membrane protein |
Biological source | Todarodes pacificus (Japanese flying squid) |
Cellular location | Membrane; Multi-pass membrane protein: P31356 |
Total number of polymer chains | 2 |
Total formula weight | 103432.12 |
Authors | Murakami, M.,Kouyama, T. (deposition date: 2007-08-13, release date: 2008-05-13, Last modification date: 2024-10-16) |
Primary citation | Murakami, M.,Kouyama, T. Crystal structure of squid rhodopsin. Nature, 453:363-367, 2008 Cited by PubMed Abstract: Invertebrate phototransduction uses an inositol-1,4,5-trisphosphate signalling cascade in which photoactivated rhodopsin stimulates a G(q)-type G protein, that is, a class of G protein that stimulates membrane-bound phospholipase Cbeta. 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 A resolution. Among seven transmembrane alpha-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 G(q)-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. PubMed: 18480818DOI: 10.1038/nature06925 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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