Early structural rearrangements in the photocycle of an integral membrane sensory receptor

Karl Edman, Antoine Royant, Peter Nollert, Carrie A. Maxwell, Eva Pebay-Peyroula, Javier Navarro, Richard Neutze, Ehud M. Landau

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


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 Å resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's β-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.

Original languageEnglish (US)
Pages (from-to)473-482
Number of pages10
Issue number4
StatePublished - 2002


  • Archael rhodopsins
  • Kinetic crystallography
  • Sensory rhodopsin II
  • Signal transduction
  • Structural intermediates
  • Structural mechanism

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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