1L9H
Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION
Summary for 1L9H
| Entry DOI | 10.2210/pdb1l9h/pdb |
| Related | 1F88 1HZX |
| Descriptor | rhodopsin, RETINAL, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total) |
| Functional Keywords | g protein-coupled receptor, membrane protein, retinal protein, photoreceptor, signaling protein |
| Biological source | Bos taurus (cattle) |
| Cellular location | Membrane; Multi-pass membrane protein: P02699 |
| Total number of polymer chains | 2 |
| Total formula weight | 86548.97 |
| Authors | Okada, T.,Fujiyoshi, Y.,Silow, M.,Navarro, J.,Landau, E.M.,Shichida, Y. (deposition date: 2002-03-23, release date: 2002-05-15, Last modification date: 2024-10-23) |
| Primary citation | Okada, T.,Fujiyoshi, Y.,Silow, M.,Navarro, J.,Landau, E.M.,Shichida, Y. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc.Natl.Acad.Sci.USA, 99:5982-5987, 2002 Cited by PubMed Abstract: Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment. PubMed: 11972040DOI: 10.1073/pnas.082666399 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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