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

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, Thomas Ve, Jason N Busby, Julie E Dalziel, J Shaun Lott, Ben Hankamer, Henning Stahlberg, Mark R H Hurst and Michael J Landsberg ()
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Sarah J Piper: The University of Queensland
Lou Brillault: 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
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

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: 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.

Date: 2019
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09890-8

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DOI: 10.1038/s41467-019-09890-8

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