Structural highlights
Function
[BACS2_NATPH] Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light.
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
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.
Early structural rearrangements in the photocycle of an integral membrane sensory receptor.,Edman K, Royant A, Nollert P, Maxwell CA, Pebay-Peyroula E, Navarro J, Neutze R, Landau EM Structure. 2002 Apr;10(4):473-82. PMID:11937052[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Edman K, Royant A, Nollert P, Maxwell CA, Pebay-Peyroula E, Navarro J, Neutze R, Landau EM. Early structural rearrangements in the photocycle of an integral membrane sensory receptor. Structure. 2002 Apr;10(4):473-82. PMID:11937052
