Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy.
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.
Department of Biochemistry, University of Cambridge, Cambridge, UK.
Antoine
A
Gautier
Helen R
HR
Mott
Mark J
MJ
Bostock
John P
JP
Kirkpatrick
Daniel
D
Nietlispach
D003902:Detergents; D006216:Halobacteriaceae / Q000737:chemistry; D025602:Halorhodopsins / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D055550:Protein Stability; D017433:Protein Structure, Secondary; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry; D025603:Sensory Rhodopsins / Q000737:chemistry*; D012995:Solubility; D013816:Thermodynamics
D003902:Detergents; D025602:Halorhodopsins; D008823:Micelles; D043562:Receptors, G-Protein-Coupled; D025603:Sensory Rhodopsins; C061508:sensory rhodopsin II protein, archaeal