9CBC

Yersinia entomophaga holotoxin complex in pore conformation

これはPDB形式変換不可エントリーです。

9CBC の概要

• エントリーDOI: 10.2210/pdb9cbc/pdb
• 関連するPDBエントリー: 9C4k
• EMDBエントリー: 45422
• 分子名称: Toxin subunit YenA1, Toxin subunit YenA2, Chitinase 2, ... (5 entities in total)
• 機能のキーワード: toxin, pore-forming, insecticidal, chitinases
• 由来する生物種: Yersinia entomophaga; 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 2054601.19

構造登録者

Low, Y.S.,Landsberg, M.J. (登録日: 2024-06-19, 公開日: 2025-12-31)

主引用文献

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

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: 41397958
DOI: 10.1038/s41467-025-66050-x

実験手法

ELECTRON MICROSCOPY (6.43 Å)