2HPY
Crystallographic model of lumirhodopsin
Summary for 2HPY
| Entry DOI | 10.2210/pdb2hpy/pdb |
| Related | 1U19 2G87 |
| Descriptor | Rhodopsin, HEPTANE-1,2,3-TRIOL, 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, visual pigment, signaling protein |
| Biological source | Bos taurus (cattle) |
| Cellular location | Membrane; Multi-pass membrane protein: P02699 |
| Total number of polymer chains | 2 |
| Total formula weight | 85393.66 |
| Authors | Nakamichi, H.,Okada, T. (deposition date: 2006-07-18, release date: 2006-08-22, Last modification date: 2024-10-30) |
| Primary citation | Nakamichi, H.,Okada, T. Local peptide movement in the photoreaction intermediate of rhodopsin Proc.Natl.Acad.Sci.Usa, 103:12729-12734, 2006 Cited by PubMed Abstract: Photoactivation of the visual rhodopsin, a prototypical G protein-coupled receptor (GPCR), involves efficient conversion of the intrinsic inverse-agonist 11-cis-retinal to the all-trans agonist. This event leads to the rearrangement of the heptahelical transmembrane bundle, which is thought to be shared by hundreds of GPCRs. To examine this activation mechanism, we determined the x-ray crystallographic model of the photoreaction intermediate of rhodopsin, lumirhodopsin, which represents the conformational state having the nearly complete all-trans agonist form of the retinal. A difference electron density map clearly indicated that the distorted all-trans-retinal in the precedent intermediate bathorhodopsin relaxes by dislocation of the beta-ionone ring in lumirhodopsin, along with significant peptide displacement in the middle of helix III, including approximately two helical turns. This local movement results in the breaking of the electrostatic interhelical restraints mediated by many of the conserved residues among rhodopsin-like GPCRs, with consequent acquisition of full activity. PubMed: 16908857DOI: 10.1073/pnas.0601765103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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