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TitleElectron crystallography reveals the structure of metarhodopsin I.
Journal, issue, pagesEMBO J, Vol. 23, Issue 18, Page 3609-3620, Year 2004
Publish dateSep 15, 2004
AuthorsJonathan J Ruprecht / Thorsten Mielke / Reiner Vogel / Claudio Villa / Gebhard F X Schertler /
PubMed AbstractRhodopsin is the prototypical G protein-coupled receptor, responsible for detection of dim light in vision. Upon absorption of a photon, rhodopsin undergoes structural changes, characterised by ...Rhodopsin is the prototypical G protein-coupled receptor, responsible for detection of dim light in vision. Upon absorption of a photon, rhodopsin undergoes structural changes, characterised by distinct photointermediates. Currently, only the ground-state structure has been described. We have determined a density map of a photostationary state highly enriched in metarhodopsin I, to a resolution of 5.5 A in the membrane plane, by electron crystallography. The map shows density for helix 8, the cytoplasmic loops, the extracellular plug, all tryptophan residues, an ordered cholesterol molecule and the beta-ionone ring. Comparison of this map with X-ray structures of the ground state reveals that metarhodopsin I formation does not involve large rigid-body movements of helices, but there is a rearrangement close to the bend of helix 6, at the level of the retinal chromophore. There is no gradual build-up of the large conformational change known to accompany metarhodopsin II formation. The protein remains in a conformation similar to that of the ground state until late in the photobleaching process.
External linksEMBO J / PubMed:15329674 / PubMed Central
MethodsEM (electron crystallography)
Resolution5.5 Å
Structure data

EMDB-1079:
Electron crystallography reveals the structure of metarhodopsin I.
Method: EM (electron crystallography) / Resolution: 5.5 Å

Source
  • Bos taurus (cattle)

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