1GUE
SENSORY RHODOPSIN II
Summary for 1GUE
| Entry DOI | 10.2210/pdb1gue/pdb |
| Related | 1GU8 1H68 1JGJ |
| Descriptor | SENSORY RHODOPSIN II, RETINAL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | archaeal rhodopsin, photoreceptor, phototaxis |
| Biological source | NATRONOMONAS PHARAONIS (NATRONOBACTERIUM PHARAONIS) |
| Cellular location | Cell membrane; Multi-pass membrane protein: P42196 |
| Total number of polymer chains | 1 |
| Total formula weight | 25688.70 |
| Authors | Edman, K.,Royant, A.,Nollert, P.,Maxwell, C.A.,Pebay-Peyroula, E.,Navarro, J.,Neutze, R.,Landau, E.M. (deposition date: 2002-01-24, release date: 2002-04-12, Last modification date: 2024-11-20) |
| Primary citation | Edman, K.,Royant, A.,Nollert, P.,Maxwell, C.A.,Pebay-Peyroula, E.,Navarro, J.,Neutze, R.,Landau, E.M. Early Structural Rearrangements in the Photocycle of an Integral Membrane Sensory Receptor Structure, 10:473-, 2002 Cited by PubMed Abstract: Sensory rhodopsins are the primary receptors of vision in animals and phototaxis in microorganisms. Light triggers the rapid isomerization of a buried retinal chromophore, which the protein both accommodates and amplifies into the larger structural rearrangements required for signaling. We trapped an early intermediate of the photocycle of sensory rhodopsin II from Natronobacterium pharaonis (pSRII) in 3D crystals and determined its X-ray structure to 2.3 A resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's beta-ionone ring undergoing a prominent movement. Comparison with the early structural rearrangements of bacteriorhodopsin illustrates how modifications in the retinal binding pocket of pSRII allow subtle differences in the early relaxation of photoisomerized retinal. PubMed: 11937052DOI: 10.1016/S0969-2126(02)00736-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
Download full validation report






