1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein from the agricultural pest Ostrinia furnacalis (OfurPBP2)
1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein from the agricultural pest Ostrinia furnacalis (OfurPBP2)
复制标题
农业害虫玉米螟信息素结合蛋白 (OfurPBP2) 的 1H、13C 和 15N 共振分配和二级结构
DOI：
10.1007/s12104-020-09930
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发表时间：
2020
影响因子：
0.9
通讯作者：
Dahal, S.
中科院分区：
文献类型：
--
作者：
Dahal, S.
亚洲玉米螟（Ostriniafurnacalis）是一种鳞翅目蛾，是一种入侵性害虫，发现于亚洲、澳大利亚、非洲和美国部分地区。 TheO。雄性蛾触角中存在的furnacalispheromone结合蛋白2 (OfurPBP2)在导致交配的过程中检测雌性分泌的信息素中发挥作用。为了了解这种害虫信息素结合和释放的结构机制，我们开始通过溶液核磁共振对 OfurPBP2 进行表征。在这里，我们使用统一 13 C, 15 N 标记的蛋白质通过各种三重共振 NMR 实验报告了 OfurPBP2 在 pH 6.5 下的主链共振分配和二级结构元件。主链任务完成了 97%，侧链共振任务完成了 88%。 OfurPBP2 的二级结构基于主链化学位移，由八个 α 螺旋组成，其中包括一个结构良好的 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. TheO. furnacalispheromone-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 uniformly13C,15N-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 α-helices, including a well-structured C-terminal helix.