9PHF

Vpb4Aa2 pore complex in C7 symmetry

9PHF の概要

• エントリーDOI: 10.2210/pdb9phf/pdb
• EMDBエントリー: 71647
• 分子名称: Vip4, CALCIUM ION (2 entities in total)
• 機能のキーワード: vpb4, vip4, bacterial toxin, pore-forming toxin, translocase, insecticidal, toxin
• 由来する生物種: Bacillus thuringiensis
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 588481.08

構造登録者

Wirawan, R.,Spicer, B.A.,Lupton, C.J.,Venugopal, H.,Berry, C.,Dunstone, M.A. (登録日: 2025-07-09, 公開日: 2026-06-24, 最終更新日: 2026-07-15)

主引用文献

Wirawan, R.,Jamieson, W.D.,Baird, H.M.,Berry, C.,Lupton, C.J.,Venugopal, H.,Valentin-Alvarado, L.E.,Best, H.L.,Jones, D.D.,Williamson, L.J.,Auhim, H.S.,Castell, O.K.,Dunstone, M.A.,Spicer, B.A.
Structural basis for independent pore function of Vpb4 from Bacillus thuringiensis.
Nat Commun, 2026

PubMed Abstract: The Bacterial_Exotoxin_B family constitutes translocating pore-forming proteins that function as the binding (B) component in the binary AB Toxin mechanism. While the two-component system of the family is consistent among well-characterised members, the single-component Vpb4 subclass from entomopathogenic Bacillus thuringiensis challenges this dogma. Here, through single-particle cryo-electron microscopy, we elucidate the inserted pore structure of a Vpb4 member, Vpb4Aa2, at 2.2 Å resolution. The structure reveals distinguishing features from other family members: missing molecular bottleneck and neutrally charged β-barrel. Accordingly, preliminary electrophysiology studies show greater ion flux by Vpb4Aa2 compared to archetypal family member, PA. Through our findings, structure-guided database search allows identification of putative Vpb4-like proteins, which suggest a broader class of single-component proteins within the larger family. This provides mechanistic understanding of the differences between independent pores and translocating pores, with implications in the agricultural industry for screening and identification of future pest control candidates.

PubMed: 42386714
DOI: 10.1038/s41467-026-74567-y

実験手法

ELECTRON MICROSCOPY (2.2 Å)