CAJ | 학술논문

采用分子对接方法研究了杀线虫苏云金芽胞杆菌晶体蛋白 Cry5Aa 与线虫糖脂受体寡糖片段的互作模式。结果表明：Cry5Aa与寡糖片段的结合位点在晶体蛋白结构域I和结构域II之间。Cry5Aa与寡糖片段的之间作用能主要为构象能，其次为氢键能，而静电作用能为零。二者之间能够形成10个氢键和多个构象能作用。其中晶体蛋白Cry5Aa结构域I氨基酸残基T298可与寡糖片段形成3个氢键，并且该氨基酸残基同样对构象能的贡献较大。Cry5Aa与寡糖片段的之间可以形成稳定的复合物。本研究结果对了解苏云金芽胞杆菌晶体蛋白Cry5Aa的毒理机制和开展定点突变提高Cry5Aa杀线虫活性具有指导意义。
채용분자대접방법연구료살선충소운금아포간균정체단백 Cry5Aa 여선충당지수체과당편단적호작모식。결과표명：Cry5Aa여과당편단적결합위점재정체단백결구역I화결구역II지간。Cry5Aa여과당편단적지간작용능주요위구상능，기차위경건능，이정전작용능위령。이자지간능구형성10개경건화다개구상능작용。기중정체단백Cry5Aa결구역I안기산잔기T298가여과당편단형성3개경건，병차해안기산잔기동양대구상능적공헌교대。Cry5Aa여과당편단적지간가이형성은정적복합물。본연구결과대료해소운금아포간균정체단백Cry5Aa적독리궤제화개전정점돌변제고Cry5Aa살선충활성구유지도의의。
Molecular docking was used to simulate the interaction between nematicidal Bacillus thuringiensis crystal protein Cry5Aa and its oligosaccharides fragment of the glycolipid receptor of target nematode. Results showed that the receptor binding site was located between domain I and domain II of Cry5Aa. The main interaction energy was the steric energy, next was the hydrogen bonding energy and the electrostatic interaction energy zero. Ten hydrogen bonds and several steric interactions were found in the binding site. Three hydrogen bonds were related to Thr298 in domain I that also contributed much to the steric energy. And as a result Cry5Aa and its receptor oligosaccharides formed a stable complex. The available results in this paper may help in understanding the action mode of Cry5Aa and designing mutagenesis experiments aimed to the improvement of nematicidal toxicity.