6ogd | pdb_00006ogd

Cryo-EM structure of YenTcA in its prepore state

Loading... Status: waiting for Mol* initialization Structural highlights 6ogd is a 15 chain structure with sequence from Yersinia entomophaga. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Chitinase, with EC number 3.2.1.14 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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). [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). [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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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