Summary


  • The structure of N2C/D282C rhodopsin is the first of a GPCR produced by recombinant DNA technology
  • Engineering of a disulfide bond lead to 10°C thermal stabilization of the receptor without changing its activity and structure
  • The ligand retinal is unlikely entering from the extracellular side, as the extracellular cap is fixed by the introduced disulfide bond
  • Micro-crystallography was applied to collect a full dataset from crystals measuring 90x5x5 µm3
  • This work is an important step towards structure determination of other medically important rhodopsin mutants and GPCRs

References

  1. Palczewski, K., et al., Crystal structure of rhodopsin: A G protein-coupled receptor. Science, 2000. 289(5480): p. 739-45.
  2. Li, J., et al., Structure of bovine rhodopsin in a trigonal crystal form. J Mol Biol, 2004. 343(5): p. 1409-38.
  3. Standfuss, J., et al., Crystal Structure of a Thermally Stable Rhodopsin Mutant. J Mol Biol, 2007: p. in press.
  4. Xie, G., A.K. Gross, and D.D. Oprian, An opsin mutant with increased thermal stability. Biochemistry, 2003. 42(7): p. 1995-2001.
  5. Cusack, S., et al., Small is beautiful: protein micro-crystallography. Nat Struct Biol, 1998. 5 Suppl: p. 634-7.
  6. Riekel, C., M. Burghammer, and G. Schertler, Protein crystallography microdiffraction. Curr Opin Struct Biol, 2005. 15(5): p. 556-62.
  7. Edwards, P.C., et al., Crystals of native and modified bovine rhodopsins and their heavy atom derivatives. J Mol Biol, 2004. 343(5): p. 1439-50.


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