6VLS

Structure of C-terminal fragment of Vip3A toxin

6VLS の概要

• エントリーDOI: 10.2210/pdb6vls/pdb
• 分子名称: Maltose/maltodextrin-binding periplasmic protein,Vip3Aa, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: bacillus thuringiensis, vip3a, biological control, mode of action, glycobiology, toxin
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 430668.41

構造登録者

Jiang, K.,Zhang, Y.,Chen, Z.,Gao, X. (登録日: 2020-01-25, 公開日: 2020-07-22, 最終更新日: 2023-10-11)

主引用文献

Jiang, K.,Zhang, Y.,Chen, Z.,Wu, D.,Cai, J.,Gao, X.
Structural and Functional Insights into the C-terminal Fragment of Insecticidal Vip3A Toxin ofBacillus thuringiensis.
Toxins, 12:-, 2020

PubMed Abstract: The vegetative insecticidal proteins (Vips) secreted by are regarded as the new generation of insecticidal toxins because they have different insecticidal properties compared with commonly applied insecticidal crystal proteins (Cry toxins). Vip3A toxin, representing the vast majority of Vips, has been used commercially in transgenic crops and bio-insecticides. However, the lack of both structural information on Vip3A and a clear understanding of its insecticidal mechanism at the molecular level limits its further development and broader application. Here we present the first crystal structure of the C-terminal fragment of Vip3A toxin (Vip3Aa11). Since all members of this insecticidal protein family are highly conserved, the structure of Vip3A provides unique insight into the general domain architecture and protein fold of the Vip3A family of insecticidal toxins. Our structural analysis reveals a four-domain organization, featuring a potential membrane insertion region, a receptor binding domain, and two potential glycan binding domains of Vip3A. In addition, cytotoxicity assays and insect bioassays show that the purified C-terminal fragment of Vip3Aa toxin alone have no insecticidal activity. Taken together, these findings provide insights into the mode of action of the Vip3A family of insecticidal toxins and will boost the development of Vip3A into more efficient bio-insecticides.

PubMed: 32635593
DOI: 10.3390/toxins12070438

実験手法

X-RAY DIFFRACTION (3.2 Å)