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  Cryo-EM structure of the native rhodopsin dimer in nanodiscs

Zhao, D. Y., Pöge, M., Morizumi, T., Gulati, S., Van Eps, N., Zhang, J., et al. (2019). Cryo-EM structure of the native rhodopsin dimer in nanodiscs. JOURNAL OF BIOLOGICAL CHEMISTRY, 294(39), 14215-14230. doi:10.1074/jbc.RA119.010089.

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Zhao, Dorothy Yanling1, Autor
Pöge, Matthias2, Autor           
Morizumi, Takefumi1, Autor
Gulati, Sahil1, Autor
Van Eps, Ned1, Autor
Zhang, Jianye1, Autor
Miszta, Przemyslaw1, Autor
Filipek, Slawomir1, Autor
Mahamid, Julia1, Autor
Plitzko, Jürgen M.2, Autor           
Baumeister, Wolfgang2, Autor           
Ernst, Oliver P.1, Autor
Palczewski, Krzysztof1, Autor
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Schlagwörter: PROTEIN-COUPLED RECEPTOR; CRYSTAL-STRUCTURE; OPIOID RECEPTOR; C5A RECEPTOR; DIMERIZATION; OLIGOMERIZATION; CELLS; OPSIN; ORGANIZATION; ARRESTING protein-coupled receptor (GPCR); receptor; rhodopsin; retinoid-binding protein; retina; cryo-electron microscopy (cryo-EM); rod outer segment; transmembrane helix 1 (TM1); helix 8 (H8); cell signaling; double electron-electron resonance (DEER); rhodopsin dimerization; transducin;
 Zusammenfassung: Imaging of rod photoreceptor outer-segment disc membranes by atomic force microscopy and cryo-electron tomography has revealed that the visual pigment rhodopsin, a prototypical class A G protein?coupled receptor (GPCR), can organize as rows of dimers. GPCR dimerization and oligomerization offer possibilities for allosteric regulation of GPCR activity, but the detailed structures and mechanism remain elusive. In this investigation, we made use of the high rhodopsin density in the native disc membranes and of a bifunctional cross-linker that preserves the native rhodopsin arrangement by covalently tethering rhodopsins via Lys residue side chains. We purified cross-linked rhodopsin dimers and reconstituted them into nanodiscs for cryo-EM analysis. We present cryo-EM structures of the cross-linked rhodopsin dimer as well as a rhodopsin dimer reconstituted into nanodiscs from purified monomers. We demonstrate the presence of a preferential 2-fold symmetrical dimerization interface mediated by transmembrane helix 1 and the cytoplasmic helix 8 of rhodopsin. We confirmed this dimer interface by double electron?electron resonance measurements of spin-labeled rhodopsin. We propose that this interface and the arrangement of two protomers is a prerequisite for the formation of the observed rows of dimers. We anticipate that the approach outlined here could be extended to other GPCRs or membrane receptors to better understand specific receptor dimerization mechanisms.

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Sprache(n): eng - English
 Datum: 2019
 Publikationsstatus: Erschienen
 Seiten: 16
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000499248200006
DOI: 10.1074/jbc.RA119.010089
 Art des Abschluß: -

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Titel: JOURNAL OF BIOLOGICAL CHEMISTRY
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Seiten: - Band / Heft: 294 (39) Artikelnummer: - Start- / Endseite: 14215 - 14230 Identifikator: ISSN: 0021-9258