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Atomic structures of amyloid cross-β spines reveal varied steric zippers

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  • Michael R. Sawaya

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Shilpa Sambashivan

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Rebecca Nelson

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Magdalena I. Ivanova

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Stuart A. Sievers

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Marcin I. Apostol

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Michael J. Thompson

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Melinda Balbirnie

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Jed J. W. Wiltzius

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Heather T. McFarlane

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

  • Anders Ø. Madsen

    (Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK-2100 KBH, Denmark
    European Synchrotron Radiation Facility, BP 220, F-38043 Grenoble Cedex, France)

  • Christian Riekel

    (European Synchrotron Radiation Facility, BP 220, F-38043 Grenoble Cedex, France)

  • David Eisenberg

    (Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA)

Abstract

Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry ‘steric zipper’. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer’s amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

Suggested Citation

  • Michael R. Sawaya & Shilpa Sambashivan & Rebecca Nelson & Magdalena I. Ivanova & Stuart A. Sievers & Marcin I. Apostol & Michael J. Thompson & Melinda Balbirnie & Jed J. W. Wiltzius & Heather T. McFar, 2007. "Atomic structures of amyloid cross-β spines reveal varied steric zippers," Nature, Nature, vol. 447(7143), pages 453-457, May.
  • Handle: RePEc:nat:nature:v:447:y:2007:i:7143:d:10.1038_nature05695
    DOI: 10.1038/nature05695
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    Cited by:

    1. Thomas Heerde & Desiree Schütz & Yu-Jie Lin & Jan Münch & Matthias Schmidt & Marcus Fändrich, 2023. "Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    2. Robert Bücker & Carolin Seuring & Cornelia Cazey & Katharina Veith & Maria García-Alai & Kay Grünewald & Meytal Landau, 2022. "The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Andreas Bittracher & Johann Moschner & Beate Koksch & Roland Netz & Christof Schütte, 2021. "Exploring the locking stage of NFGAILS amyloid fibrillation via transition manifold analysis," The European Physical Journal B: Condensed Matter and Complex Systems, Springer;EDP Sciences, vol. 94(10), pages 1-12, October.
    4. Lukas Frey & Jiangtao Zhou & Gea Cereghetti & Marco E. Weber & David Rhyner & Aditya Pokharna & Luca Wenchel & Harindranath Kadavath & Yiping Cao & Beat H. Meier & Matthias Peter & Jason Greenwald & R, 2024. "A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    5. Dániel Horváth & Zsolt Dürvanger & Dóra K. Menyhárd & Máté Sulyok-Eiler & Fruzsina Bencs & Gergő Gyulai & Péter Horváth & Nóra Taricska & András Perczel, 2023. "Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    6. Einav Tayeb-Fligelman & Jeannette T. Bowler & Christen E. Tai & Michael R. Sawaya & Yi Xiao Jiang & Gustavo Garcia & Sarah L. Griner & Xinyi Cheng & Lukasz Salwinski & Liisa Lutter & Paul M. Seidler &, 2023. "Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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