8HHE

Crystal structure of Cry5B from Bacillus thuringiensis at 4.5 A resolution

8HHE の概要

• エントリーDOI: 10.2210/pdb8hhe/pdb
• 分子名称: Crystaline entomocidal protoxin (1 entity in total)
• 機能のキーワード: bacillus thuringiensis, cry protein, nematicidal protein, toxin
• 由来する生物種: Bacillus thuringiensis YBT-1518
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 181221.66

構造登録者

Li, J.,Chan, M.K. (登録日: 2022-11-16, 公開日: 2022-12-07, 最終更新日: 2024-11-06)

主引用文献

Li, J.,Wang, L.,Kotaka, M.,Lee, M.M.,Chan, M.K.
Insights from the Structure of an Active Form of Bacillus thuringiensis Cry5B.
Toxins, 14:-, 2022

PubMed Abstract: The crystal protein Cry5B, a pore-forming protein produced by the soil bacterium , has been demonstrated to have excellent anthelmintic activity. While a previous structure of the three-domain core region of Cry5B(112-698) had been reported, this structure lacked a key N-terminal extension critical to function. Here we report the structure of Cry5B(27-698) containing this N-terminal extension. This new structure adopts a distinct quaternary structure compared to the previous Cry5B(112-698) structure, and also exhibits a change in the conformation of residues 112-140 involved in linking the N-terminal extension to the three-domain core by forming a random coil and an extended α-helix. A role for the N-terminal extension is suggested based on a computational model of the tetramer with the conformation of residues 112-140 in its alternate α-helix conformation. Finally, based on the Cry5B(27-698) structure, site-directed mutagenesis studies were performed on Tyr495, which revealed that having an aromatic group or bulky group at this residue 495 is important for Cry5B toxicity.

PubMed: 36548720
DOI: 10.3390/toxins14120823

実験手法

X-RAY DIFFRACTION (4.5 Å)