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ProteomicsComplete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins
ABC toxins are toxin-translocating, pore-forming proteins found in a wide range of insecticidal bacteria and some mammalian pathogens. The Yersinia entomopahaga toxin complex (YenTc) belongs to a distinct subclass of ABC toxins, defined by a divergent molecular architecture. Structural details that ...
ORGANISM(S): Yersinia entomophaga 
2025-12-22 | PXD068275 | Pride
Yentc Xlms Pores Abc toxins Alphafold Cryoem 
UnknownComplete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.
Not available
S-EPMC12705794 | biostudies-literature
UnknownStepwise assembly and release of Tc toxins from Yersinia entomophaga.
Not available
S-EPMC10847046 | biostudies-literature
ProteomicsAssembly and release of a Tc toxin
Tripartite Tc toxins are virulence factors of bacterial pathogens. Although their structure and mechanism of action are well understood, it remains elusive where this large macromolecular complex is assembled and how it is released. Here we show by an integrative multiscale imaging approach that Yer...
ORGANISM(S): Yersinia entomophaga 
2024-02-20 | PXD048008 | Pride
Toxins 
ProteomicsComparison of secreted to non-secreted proteins of Y. entomophaga
Identification the proteins co-secreted with YenTc and compare them to those remaining in yersinia entomophaga cells by bottom-up proteomics.
ORGANISM(S): Yersinia Entomophaga (ncbitaxon:935293) 
2022-07-25 | MSV000089961 | MassIVE
UnknownCryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin.
Not available
S-EPMC6486591 | biostudies-literature
UnknownYersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations.
Not available
S-EPMC10847048 | biostudies-literature
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