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Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

Author

Listed:
  • Sarah J Piper

    (The University of Queensland
    The University of Queensland)

  • Lou Brillault

    (The University of Queensland
    The University of Queensland)

  • Rosalba Rothnagel

    (The University of Queensland)

  • Tristan I Croll

    (University of Cambridge)

  • Joseph K Box

    (The University of Queensland)

  • Irene Chassagnon

    (The University of Queensland)

  • Sebastian Scherer

    (University of Basel)

  • Kenneth N Goldie

    (University of Basel)

  • Sandra A Jones

    (AgResearch)

  • Femke Schepers

    (Leiden University
    AgResearch)

  • Lauren Hartley-Tassell

    (Griffith University)

  • Thomas Ve

    (Griffith University)

  • Jason N Busby

    (University of Auckland)

  • Julie E Dalziel

    (AgResearch)

  • J Shaun Lott

    (University of Auckland)

  • Ben Hankamer

    (The University of Queensland)

  • Henning Stahlberg

    (University of Basel)

  • Mark R H Hurst

    (AgResearch)

  • Michael J Landsberg

    (The University of Queensland
    The University of Queensland)

Abstract

ABC toxins are pore-forming virulence factors produced by pathogenic bacteria. YenTcA is the pore-forming and membrane binding A subunit of the ABC toxin YenTc, produced by the insect pathogen Yersinia entomophaga. Here we present cryo-EM structures of YenTcA, purified from the native source. The soluble pre-pore structure, determined at an average resolution of 4.4 Å, reveals a pentameric assembly that in contrast to other characterised ABC toxins is formed by two TcA-like proteins (YenA1 and YenA2) and decorated by two endochitinases (Chi1 and Chi2). We also identify conformational changes that accompany membrane pore formation by visualising YenTcA inserted into liposomes. A clear outward rotation of the Chi1 subunits allows for access of the protruding translocation pore to the membrane. Our results highlight structural and functional diversity within the ABC toxin subfamily, explaining how different ABC toxins are capable of recognising diverse hosts.

Suggested Citation

  • Sarah J Piper & Lou Brillault & Rosalba Rothnagel & Tristan I Croll & Joseph K Box & Irene Chassagnon & Sebastian Scherer & Kenneth N Goldie & Sandra A Jones & Femke Schepers & Lauren Hartley-Tassell , 2019. "Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09890-8
    DOI: 10.1038/s41467-019-09890-8
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