| Structural highlights
Function
[YENA1_YERET] Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295, PubMed:22158901). The TC has an endochitinase activity (PubMed:21278295) (Probable).[1] [2] [3] [CHI2_YERET] Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295). The TC has an endochitinase activity (PubMed:21278295, PubMed:22158901) (Probable). This subunit might aid infection by degradation of the larval peritrophic membrane (Probable).[4] [5] [6] [YENA2_YERET] Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295, PubMed:22158901). The TC has an endochitinase activity (PubMed:21278295) (Probable).[7] [8] [9]
Publication Abstract from PubMed
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 A, 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.
Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin.,Piper SJ, Brillault L, Rothnagel R, Croll TI, Box JK, Chassagnon I, Scherer S, Goldie KN, Jones SA, Schepers F, Hartley-Tassell L, Ve T, Busby JN, Dalziel JE, Lott JS, Hankamer B, Stahlberg H, Hurst MRH, Landsberg MJ Nat Commun. 2019 Apr 26;10(1):1952. doi: 10.1038/s41467-019-09890-8. PMID:31028251[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hurst MR, Jones SA, Binglin T, Harper LA, Jackson TA, Glare TR. The main virulence determinant of Yersinia entomophaga MH96 is a broad-host-range toxin complex active against insects. J Bacteriol. 2011 Apr;193(8):1966-80. doi: 10.1128/JB.01044-10. Epub 2011 Jan 28. PMID:21278295 doi:http://dx.doi.org/10.1128/JB.01044-10
- ↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
- ↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
- ↑ Hurst MR, Jones SA, Binglin T, Harper LA, Jackson TA, Glare TR. The main virulence determinant of Yersinia entomophaga MH96 is a broad-host-range toxin complex active against insects. J Bacteriol. 2011 Apr;193(8):1966-80. doi: 10.1128/JB.01044-10. Epub 2011 Jan 28. PMID:21278295 doi:http://dx.doi.org/10.1128/JB.01044-10
- ↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
- ↑ Busby JN, Landsberg MJ, Simpson R, Jones SA, Hankamer B, Hurst MR, Lott JS. Structural Analysis of Chi1 Chitinase from Yen-Tc: The Multisubunit Insecticidal ABC Toxin Complex of Yersinia entomophaga. J Mol Biol. 2011 Nov 15. PMID:22108167 doi:10.1016/j.jmb.2011.11.018
- ↑ Hurst MR, Jones SA, Binglin T, Harper LA, Jackson TA, Glare TR. The main virulence determinant of Yersinia entomophaga MH96 is a broad-host-range toxin complex active against insects. J Bacteriol. 2011 Apr;193(8):1966-80. doi: 10.1128/JB.01044-10. Epub 2011 Jan 28. PMID:21278295 doi:http://dx.doi.org/10.1128/JB.01044-10
- ↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
- ↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
- ↑ Piper SJ, Brillault L, Rothnagel R, Croll TI, Box JK, Chassagnon I, Scherer S, Goldie KN, Jones SA, Schepers F, Hartley-Tassell L, Ve T, Busby JN, Dalziel JE, Lott JS, Hankamer B, Stahlberg H, Hurst MRH, Landsberg MJ. Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin. Nat Commun. 2019 Apr 26;10(1):1952. doi: 10.1038/s41467-019-09890-8. PMID:31028251 doi:http://dx.doi.org/10.1038/s41467-019-09890-8
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