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

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

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1
Department of Biochemistry, University of Cambridge, Cambridge, UK.

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.

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PMID:
20512150
PMCID:
PMC2923064
DOI:
10.1038/nsmb.1807
[Indexed for MEDLINE]
Free PMC Article
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