Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein

Nat Methods. 2013 Oct;10(10):1007-12. doi: 10.1038/nmeth.2635. Epub 2013 Sep 8.


Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning solid-state NMR spectroscopy can be used to determine structures of membrane proteins reconstituted in synthetic lipids, an environment similar to the natural membrane. We combined a large number of experimentally determined interatomic distances and local torsional restraints to solve the structure of an oligomeric membrane protein of common seven-helical fold, Anabaena sensory rhodopsin (ASR). We determined the atomic resolution detail of the oligomerization interface of the ASR trimer, and the arrangement of helices, side chains and the retinal cofactor in the monomer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anabaena / chemistry*
  • Crystallography, X-Ray
  • Lipids / chemistry*
  • Membrane Proteins / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Multimerization
  • Sensory Rhodopsins / chemistry*


  • Lipids
  • Membrane Proteins
  • Sensory Rhodopsins

Associated data

  • PDB/2M3G