2ziy | pdb_00002ziy

Crystal structure of squid rhodopsin

spinqualitylabelsall models 2ziy, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ziy is a 1 chain structure with sequence from Todarodes pacificus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.7Å Ligands: PLM, RET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OPSD_TODPA Visual pigments such as rhodopsin and porphyropsin are light-absorbing molecules that mediate vision. Rhodopsin consists of an apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor is coupled to the activation of phospholipase C. Porphyropsin consists of opsin covalently linked to 11-cis 3,4-didehydroretinal. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed G-protein-coupled receptors play a key step in cellular signal transduction cascades by transducing various extracellular signals via G-proteins. Rhodopsin is a prototypical G-protein-coupled receptor involved in the retinal visual signaling cascade. We determined the structure of squid rhodopsin at 3.7A resolution, which transduces signals through the G(q) protein to the phosphoinositol cascade. The structure showed seven transmembrane helices and an amphipathic helix H8 has similar geometry to structures from bovine rhodopsin, coupling to G(t), and human beta(2)-adrenergic receptor, coupling to G(s). Notably, squid rhodopsin contains a well structured cytoplasmic region involved in the interaction with G-proteins, and this region is flexible or disordered in bovine rhodopsin and human beta(2)-adrenergic receptor. The transmembrane helices 5 and 6 are longer and extrude into the cytoplasm. The distal C-terminal tail contains a short hydrophilic alpha-helix CH after the palmitoylated cysteine residues. The residues in the distal C-terminal tail interact with the neighboring residues in the second cytoplasmic loop, the extruded transmembrane helices 5 and 6, and the short helix H8. Additionally, the Tyr-111, Asn-87, and Asn-185 residues are located within hydrogen-bonding distances from the nitrogen atom of the Schiff base. Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region.,Shimamura T, Hiraki K, Takahashi N, Hori T, Ago H, Masuda K, Takio K, Ishiguro M, Miyano M J Biol Chem. 2008 Jun 27;283(26):17753-6. Epub 2008 May 6. PMID:18463093 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Rhodopsin 3D structures

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