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Crystal structure of opsin in its G-protein-interacting conformation

Author

Listed:
  • Patrick Scheerer

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

  • Jung Hee Park

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

  • Peter W. Hildebrand

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

  • Yong Ju Kim

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

  • Norbert Krauß

    (Queen Mary, University of London, School of Biological and Chemical Sciences)

  • Hui-Woog Choe

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
    College of Natural Science, Chonbuk National University)

  • Klaus Peter Hofmann

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
    Zentrum für Biophysik und Bioinformatik, Humboldt-Universität zu Berlin, Invalidenstrasse 42, D-10115 Berlin, Germany)

  • Oliver P. Ernst

    (Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany)

Abstract

Opsin, the ligand-free form of the G-protein-coupled receptor rhodopsin, at low pH adopts a conformationally distinct, active G-protein-binding state known as Ops*. A synthetic peptide derived from the main binding site of the heterotrimeric G protein—the carboxy terminus of the α-subunit (GαCT)—stabilizes Ops*. Here we present the 3.2 Å crystal structure of the bovine Ops*–GαCT peptide complex. GαCT binds to a site in opsin that is opened by an outward tilt of transmembrane helix (TM) 6, a pairing of TM5 and TM6, and a restructured TM7–helix 8 kink. Contacts along the inner surface of TM5 and TM6 induce an α-helical conformation in GαCT with a C-terminal reverse turn. Main-chain carbonyl groups in the reverse turn constitute the centre of a hydrogen-bonded network, which links the two receptor regions containing the conserved E(D)RY and NPxxY(x)5,6F motifs. On the basis of the Ops*–GαCT structure and known conformational changes in Gα, we discuss signal transfer from the receptor to the G protein nucleotide-binding site.

Suggested Citation

  • Patrick Scheerer & Jung Hee Park & Peter W. Hildebrand & Yong Ju Kim & Norbert Krauß & Hui-Woog Choe & Klaus Peter Hofmann & Oliver P. Ernst, 2008. "Crystal structure of opsin in its G-protein-interacting conformation," Nature, Nature, vol. 455(7212), pages 497-502, September.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7212:d:10.1038_nature07330
    DOI: 10.1038/nature07330
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    Cited by:

    1. Valérie Capra & Marta Busnelli & Alessandro Perenna & Manuela Ambrosio & Maria Rosa Accomazzo & Celine Galés & Bice Chini & G Enrico Rovati, 2013. "Full and Partial Agonists of Thromboxane Prostanoid Receptor Unveil Fine Tuning of Receptor Superactive Conformation and G Protein Activation," PLOS ONE, Public Library of Science, vol. 8(3), pages 1-12, March.
    2. Marie Mi Bonde & Jonas Tind Hansen & Samra Joke Sanni & Stig Haunsø & Steen Gammeltoft & Christina Lyngsø & Jakob Lerche Hansen, 2010. "Biased Signaling of the Angiotensin II Type 1 Receptor Can Be Mediated through Distinct Mechanisms," PLOS ONE, Public Library of Science, vol. 5(11), pages 1-15, November.

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