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

Patrick Scheerer, Jung Hee Park, Peter W. Hildebrand, Yong Ju Kim, Norbert Krauß, Hui-Woog Choe (), Klaus Peter Hofmann () and Oliver P. Ernst ()
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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
Klaus Peter Hofmann: Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
Oliver P. Ernst: Institut für Medizinische Physik und Biophysik (CC2), Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany

Nature, 2008, vol. 455, issue 7212, 497-502

Abstract: 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.

Date: 2008
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DOI: 10.1038/nature07330

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