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Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

Author

Listed:
  • Yanyong Kang

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • X. Edward Zhou

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Xiang Gao

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Yuanzheng He

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Wei Liu

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Andrii Ishchenko

    (Bridge Institute, University of Southern California)

  • Anton Barty

    (Center for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • Thomas A. White

    (Center for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • Oleksandr Yefanov

    (Center for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • Gye Won Han

    (Bridge Institute, University of Southern California)

  • Qingping Xu

    (Joint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory)

  • Parker W. de Waal

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Jiyuan Ke

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • M. H. Eileen Tan

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute
    Yong Loo Lin School of Medicine, National University of Singapore)

  • Chenghai Zhang

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Arne Moeller

    (The National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

  • Graham M. West

    (The Scripps Research Institute, Scripps Florida)

  • Bruce D. Pascal

    (The Scripps Research Institute, Scripps Florida)

  • Ned Van Eps

    (University of California
    †Present address: Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.)

  • Lydia N. Caro

    (University of Toronto)

  • Sergey A. Vishnivetskiy

    (Vanderbilt University)

  • Regina J. Lee

    (Vanderbilt University)

  • Kelly M. Suino-Powell

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Xin Gu

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Kuntal Pal

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Jinming Ma

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Xiaoyong Zhi

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • Sébastien Boutet

    (Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory)

  • Garth J. Williams

    (Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory)

  • Marc Messerschmidt

    (Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory
    BioXFEL, NSF Science and Technology Center)

  • Cornelius Gati

    (Center for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • Nadia A. Zatsepin

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Dingjie Wang

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Daniel James

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Shibom Basu

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Shatabdi Roy-Chowdhury

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Chelsie E. Conrad

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Jesse Coe

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Haiguang Liu

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Beijing Computational Science Research Center, Haidian District)

  • Stella Lisova

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Christopher Kupitz

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    University of Wisconsin-Milwaukee)

  • Ingo Grotjohann

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Raimund Fromme

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Yi Jiang

    (State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Minjia Tan

    (State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Huaiyu Yang

    (State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Jun Li

    (Yong Loo Lin School of Medicine, National University of Singapore)

  • Meitian Wang

    (Swiss Light Source at Paul Scherrer Institute)

  • Zhong Zheng

    (Bridge Institute, University of Southern California)

  • Dianfan Li

    (School of Medicine and School of Biochemistry and Immunology, Trinity College)

  • Nicole Howe

    (School of Medicine and School of Biochemistry and Immunology, Trinity College)

  • Yingming Zhao

    (BioXFEL, NSF Science and Technology Center
    University of Chicago)

  • Jörg Standfuss

    (Laboratory of Biomolecular Research at Paul Scherrer Institute)

  • Kay Diederichs

    (Universität Konstanz)

  • Yuhui Dong

    (Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences)

  • Clinton S. Potter

    (The National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

  • Bridget Carragher

    (The National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

  • Martin Caffrey

    (School of Medicine and School of Biochemistry and Immunology, Trinity College)

  • Hualiang Jiang

    (State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Henry N. Chapman

    (Center for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
    Centre for Ultrafast Imaging)

  • John C. H. Spence

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Petra Fromme

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University)

  • Uwe Weierstall

    (and Center for Applied Structural Discovery, Biodesign Institute, Arizona State University
    Arizona State University)

  • Oliver P. Ernst

    (University of Toronto
    University of Toronto)

  • Vsevolod Katritch

    (Bridge Institute, University of Southern California)

  • Vsevolod V. Gurevich

    (Vanderbilt University)

  • Patrick R. Griffin

    (The Scripps Research Institute, Scripps Florida)

  • Wayne L. Hubbell

    (University of California)

  • Raymond C. Stevens

    (Bridge Institute, University of Southern California
    Bridge Institute, University of Southern California
    iHuman Institute, ShanghaiTech University)

  • Vadim Cherezov

    (Bridge Institute, University of Southern California)

  • Karsten Melcher

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute)

  • H. Eric Xu

    (Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute
    VARI-SIMM Center, Center for Structure and Function of Drug Targets, CAS-Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

Abstract

G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways. Here we report the crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin, determined by serial femtosecond X-ray laser crystallography. Together with extensive biochemical and mutagenesis data, the structure reveals an overall architecture of the rhodopsin–arrestin assembly in which rhodopsin uses distinct structural elements, including transmembrane helix 7 and helix 8, to recruit arrestin. Correspondingly, arrestin adopts the pre-activated conformation, with a ∼20° rotation between the amino and carboxy domains, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. This structure provides a basis for understanding GPCR-mediated arrestin-biased signalling and demonstrates the power of X-ray lasers for advancing the frontiers of structural biology.

Suggested Citation

  • Yanyong Kang & X. Edward Zhou & Xiang Gao & Yuanzheng He & Wei Liu & Andrii Ishchenko & Anton Barty & Thomas A. White & Oleksandr Yefanov & Gye Won Han & Qingping Xu & Parker W. de Waal & Jiyuan Ke & , 2015. "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser," Nature, Nature, vol. 523(7562), pages 561-567, July.
    • Handle: RePEc:nat:nature:v:523:y:2015:i:7562:d:10.1038_nature14656
    DOI: 10.1038/nature14656
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    Citations

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    Cited by:

    1. Fenghui Zhao & Qingtong Zhou & Zhaotong Cong & Kaini Hang & Xinyu Zou & Chao Zhang & Yan Chen & Antao Dai & Anyi Liang & Qianqian Ming & Mu Wang & Li-Nan Chen & Peiyu Xu & Rulve Chang & Wenbo Feng & T, 2022. "Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Raphael S. Haider & Edda S. F. Matthees & Julia Drube & Mona Reichel & Ulrike Zabel & Asuka Inoue & Andy Chevigné & Cornelius Krasel & Xavier Deupi & Carsten Hoffmann, 2022. "β-arrestin1 and 2 exhibit distinct phosphorylation-dependent conformations when coupling to the same GPCR in living cells," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    3. Kevin M. Dalton & Jack B. Greisman & Doeke R. Hekstra, 2022. "A unifying Bayesian framework for merging X-ray diffraction data," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    4. Yasmin Aydin & Thore Böttke & Jordy Homing Lam & Stefan Ernicke & Anna Fortmann & Maik Tretbar & Barbara Zarzycka & Vsevolod V. Gurevich & Vsevolod Katritch & Irene Coin, 2023. "Structural details of a Class B GPCR-arrestin complex revealed by genetically encoded crosslinkers in living cells," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    5. Yutaro Shiraishi & Yutaka Kofuku & Takumi Ueda & Shubhi Pandey & Hemlata Dwivedi-Agnihotri & Arun K. Shukla & Ichio Shimada, 2021. "Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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