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Showing 1–5 of 5 results
Advanced filters: Author: J Shaun Lott Clear advanced filters

  • The crystal structure of the complex formed by the B and C toxin complex proteins is reported, revealing how toxin complexes are processed and protected; the proteins assemble to form a large hollow structure that sequesters the cytotoxic portion of the C protein, and a β-propeller domain mediates attachment to the A protein in the native ABC complex.

    • Jason N. Busby
    • Santosh Panjikar
    • J. Shaun Lott
    Research
    Nature
    Volume: 501, P: 547-550

  • Previous studies of Teneurins identified an uncharacterized family of Teneurin-like proteins in bacteria. Here, the authors show these proteins are widespread across both Gram groups but limited to certain species, where they form barrel-like structures that encapsulate a toxin and are co-expressed with potent immunity genes.

    • Finaritra Raoelijaona
    • Joanna Szczepaniak
    • Elena Seiradake
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-14

  • ABC toxins are bacterial insecticides with biotechnological potential. Here, Low et al. have deciphered soluble and membrane-inserted structures of YenTc that highlight structural and mechanistic diversity in the ABC toxin family and provide insights into their evolution.

    • Yu Shang Low
    • Solace G. Roche
    • Michael J. Landsberg
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • YenTcA is the pore-forming and membrane binding subunit of the ABC toxin YenTc, which is produced by the insect pathogen Yersinia entomophaga. Here authors present cryo-EM structures of YenTcA purified from the native source which implicate associated endochitinases in host cell recognition.

    • Sarah J Piper
    • Lou Brillault
    • Michael J Landsberg
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12