Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy

Nat Struct Mol Biol. 2010 Jun;17(6):768-74. doi: 10.1038/nsmb.1807. Epub 2010 May 30.


Seven-helix membrane proteins represent a challenge for structural biology. Here we report the first NMR structure determination of a detergent-solubilized seven-helix transmembrane (7TM) protein, the phototaxis receptor sensory rhodopsin II (pSRII) from Natronomonas pharaonis, as a proof of principle. The overall quality of the structure ensemble is good (backbone r.m.s. deviation of 0.48 A) and agrees well with previously determined X-ray structures. Furthermore, measurements in more native-like small phospholipid bicelles indicate that the protein structure is the same as in detergent micelles, suggesting that environment-specific effects are minimal when using mild detergents. We use our case study as a platform to discuss the feasibility of similar solution NMR studies for other 7TM proteins, including members of the family of G protein-coupled receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Detergents
  • Halobacteriaceae / chemistry
  • Halorhodopsins / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Micelles
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Stability
  • Protein Structure, Secondary
  • Receptors, G-Protein-Coupled / chemistry
  • Sensory Rhodopsins / chemistry*
  • Solubility
  • Thermodynamics


  • Detergents
  • Halorhodopsins
  • Micelles
  • Receptors, G-Protein-Coupled
  • Sensory Rhodopsins
  • sensory rhodopsin II protein, archaeal