1H, 13C, and 15N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2)
1H, 13C, and 15N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2)
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DOI：
10.1007/s12104-020-09930-1
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发表时间：
2020-04-01
影响因子：
0.9
通讯作者：
Mohanty, Smita
中科院分区：
文献类型：
--
作者：
Dahal, Salik R.;Lewellen, Jacob L.;Mohanty, Smita
卷叶蛾是一种鳞翅目蛾，是一种在亚洲、澳大利亚、非洲和美国部分地区发现的入侵性害虫。手术雄蛾触角中的信息素结合蛋白2（OfurPBP 2）在雌蛾交配过程中检测雌蛾分泌的信息素中起重要作用。为了了解这种害虫的信息素结合和释放的结构机制，我们已经开始通过溶液NMR表征OfurPBP 2。在这里，我们报告的骨干共振分配和二级结构元素OfurPBP 2在pH 6.5使用均匀的C-13，N-15标记的蛋白质与各种三重共振NMR实验。主链的归属完成了97%，侧链共振的归属完成了88%。基于主链化学位移，OfurPBP 2的二级结构由八个α-螺旋组成，包括结构良好的C-末端螺旋。
Ostrinia furnacalis, a lepidopteran moth, is an invasive pest found in Asia, Australia, Africa, and parts of the United States. The O. furnacalis pheromone-binding protein2 (OfurPBP2), present in the male moth antenna, plays a role in the detection of female-secreted pheromone in a process that leads to mating. To understand the structural mechanism of pheromone binding and release in this pest, we have initiated characterization of OfurPBP2 by solution NMR. Here, we report the backbone resonance assignments and the secondary structural elements of OfurPBP2 at pH 6.5 using uniformly C-13, N-15-labeled protein with various triple resonance NMR experiments. The assignments are 97% completed for backbone and 88% completed for side-chain resonances. The secondary structure of OfurPBP2, based on backbone chemical shifts, consists of eight alpha-helices, including a well-structured C-terminal helix.