9EA9

Crystal structure of BoNT/A-NTNH-HA70 -VHH_F12-VHH_H7-Fab_NTNH complex

これはPDB形式変換不可エントリーです。

9EA9 の概要

• エントリーDOI: 10.2210/pdb9ea9/pdb
• 分子名称: Botulinum neurotoxin type A, anti-NTNH Fab, SULFATE ION, ... (14 entities in total)
• 機能のキーワード: botulinum neurotoxin, progenitor toxin complex (ptc), toxin, toxin-immune system complex, toxin/immune system
• 由来する生物種: Clostridium botulinum; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 790107.88

構造登録者

Lam, K.H.,Gao, L.,Jin, R. (登録日: 2024-11-10, 公開日: 2025-09-17)

主引用文献

Lam, K.H.,Gao, L.,Przykopanski, A.,Chen, B.,Huang, T.,Kruger, M.,Bartels, A.M.,Dorner, M.B.,Perry, K.,Dorner, B.G.,Rummel, A.,Jin, R.
A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex.
Sci Adv, 11:eadx5831-, 2025

PubMed Abstract: Botulinum neurotoxin serotype A (BoNT/A) is naturally produced by bacteria along with four nontoxic neurotoxin-associated proteins (NTNH, HA70, HA33, and HA17), forming a bimodular large progenitor toxin complex (L-PTC). The BoNT/A-NTNH complex protects the toxin from adverse environment, while the complex consisting of HA proteins facilitates toxin absorption during oral intoxication. How these two independent modules assemble into the L-PTC remains unclear. Here, we report the crystal structure of the BoNT/A-NTNH-HA70 complex at ~2.9-Å resolution. The structure reveals that the BoNT/A-NTNH complex is anchored into a concentric double β-barrel channel of trimeric HA70 through a short β-hairpin of NTNH (termed nLoop), resembling a nut-and-bolt attachment. We find that the nLoop of NTNH is strictly conserved across HA-containing BoNT complexes and that NTNH-HA70 binding is interchangeable among them. Furthermore, we demonstrate that the nLoop functions as a minimal motif enabling attachment of a protein-of-interest to the HA complex, with potential applications in oral biologics delivery.

PubMed: 40864694
DOI: 10.1126/sciadv.adx5831

実験手法

X-RAY DIFFRACTION (2.93 Å)