9C4K
Yersinia entomophaga holotoxin complex in prepore conformation
This is a non-PDB format compatible entry.
Summary for 9C4K
| Entry DOI | 10.2210/pdb9c4k/pdb |
| EMDB information | 45190 |
| Descriptor | Toxin subunit YenA1, Toxin subunit YenA2, Chitinase 2, ... (5 entities in total) |
| Functional Keywords | toxin, pore-forming, insecticidal, chitinases |
| Biological source | Yersinia entomophaga More |
| Total number of polymer chains | 17 |
| Total formula weight | 2054601.19 |
| Authors | |
| Primary citation | Low, Y.S.,Roche, S.G.,Aleksandrova, N.A.,Foley, G.,Low, J.K.,Box, J.K.,Croll, T.I.,Chassagnon, I.R.,Lott, J.S.,Deplazes, E.,Boden, M.,Hurst, M.R.,Piper, S.J.,Landsberg, M.J. Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins. Nat Commun, 16:11121-11121, 2025 Cited by PubMed Abstract: 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 define their mechanism of action remain to be elucidated. Here we determine structures of the YenTc holotoxin assembly in both prepore and pore-forming configurations using cryo-EM in conjunction with Alphafold2-assisted structural modelling of flexible domains. We define the structural mechanism via which enzymatically-active chitinase subunits are incorporated, and show using phylogenetic analyses that this subclass-defining feature has evolved relatively recently. Our structures point to the existence of distinct conformational states in YenTc, which may distinguish it from other structurally-characterised ABC toxins, or represent states on a shared mechanistic trajectory. Thus, our findings enhance our understanding of the structural diversity that defines distinct ABC toxin subclasses. PubMed: 41397958DOI: 10.1038/s41467-025-66050-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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