Download MendeleyStructure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy.
Gautier, A., Mott, H.R., Bostock, M.J., Kirkpatrick, J.P., Nietlispach, D.(2010) Nat Struct Mol Biol 17: 768-774
- PubMed: 20512150
- DOI: https://doi.org/10.1038/nsmb.1807
- Primary Citation of Related Structures:
2KSY - PubMed Abstract:
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.
Organizational Affiliation:
Department of Biochemistry, University of Cambridge, Cambridge, UK.
