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Title3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 108, Issue 51, Page 20544-20549, Year 2011
Publish dateDec 20, 2011
AuthorsMichael J Landsberg / Sandra A Jones / Rosalba Rothnagel / Jason N Busby / Sean D G Marshall / Robert M Simpson / J Shaun Lott / Ben Hankamer / Mark R H Hurst /
PubMed AbstractToxin complex (Tc) proteins are a class of bacterial protein toxins that form large, multisubunit complexes. Comprising TcA, B, and C components, they are of great interest because many exhibit ...Toxin complex (Tc) proteins are a class of bacterial protein toxins that form large, multisubunit complexes. Comprising TcA, B, and C components, they are of great interest because many exhibit potent insecticidal activity. Here we report the structure of a novel Tc, Yen-Tc, isolated from the bacterium Yersinia entomophaga MH96, which differs from the majority of bacterially derived Tcs in that it exhibits oral activity toward a broad range of insect pests, including the diamondback moth (Plutella xylostella). We have determined the structure of the Yen-Tc using single particle electron microscopy and studied its mechanism of toxicity by comparative analyses of two variants of the complex exhibiting different toxicity profiles. We show that the A subunits form the basis of a fivefold symmetric assembly that differs substantially in structure and subunit arrangement from its most well characterized homologue, the Xenorhabdus nematophila toxin XptA1. Histopathological and quantitative dose response analyses identify the B and C subunits, which map to a single, surface-accessible region of the structure, as the sole determinants of toxicity. Finally, we show that the assembled Yen-Tc has endochitinase activity and attribute this to putative chitinase subunits that decorate the surface of the TcA scaffold, an observation that may explain the oral toxicity associated with the complex.
External linksProc Natl Acad Sci U S A / PubMed:22158901 / PubMed Central
MethodsEM (single particle)
Resolution17.0 Å
Structure data

EMDB-1978:
3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity
Method: EM (single particle) / Resolution: 17.0 Å

Source
  • Yersinia entomophaga (bacteria)

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