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2Z73

Crystal structure of squid rhodopsin

Summary for 2Z73
Entry DOI10.2210/pdb2z73/pdb
DescriptorRhodopsin, octyl beta-D-glucopyranoside, RETINAL, ... (8 entities in total)
Functional Keywordsvisual 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 sourceTodarodes pacificus (Japanese flying squid)
Cellular locationMembrane; Multi-pass membrane protein: P31356
Total number of polymer chains2
Total formula weight103432.12
Authors
Murakami, M.,Kouyama, T. (deposition date: 2007-08-13, release date: 2008-05-13, Last modification date: 2024-10-16)
Primary citationMurakami, 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: 18480818
DOI: 10.1038/nature06925
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

건을2024-10-30부터공개중

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