Crystal structure of the Locusta migratoria odorant binding protein.
Crystal structure of the Locusta migratoria odorant binding protein.
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DOI：
10.1016/j.bbrc.2014.12.048
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发表时间：
2015-01
影响因子：
3.1
通讯作者：
Jiangge Zheng;Junru Li;Lei Han;Yang Wang;Wei Wu;Xiaoxuan Qi;Ye Tao;Long Zhang;Ziding Zhang-Zid
中科院分区：
文献类型：
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作者：
Jiangge Zheng;Junru Li;Lei Han;Yang Wang;Wei Wu;Xiaoxuan Qi;Ye Tao;Long Zhang;Ziding Zhang-Zid
飞蝗（Locusta migratoria，Lmig）是一种严重危害农业生产的蝗虫，在世界范围内造成了巨大的损失。蝗虫通过嗅觉系统寻找寄主植物，嗅觉系统中气味结合蛋白（OBP）起着重要作用。前期研究表明，LmigOBP的氨基酸序列与其他昆虫目的OBP相似性较低，推测其可能具有独特的结合行为。在这里，我们在1.65 nm处解析了第一个LmigOBP1结构，它是溶液中的单体，二硫键在维持其功能方面起着关键作用。我们发现LmigOBP1具有独特的第七个α-螺旋，它位于表面，与由其他六个α-螺旋组成的LmigOBP1支架有很强的相互作用。此外，第七个α-螺旋形成"L"形内部疏水腔的壁以容纳线性配体，这与结合实验一致。我们还表明，LmigOBP1中的配体结合口袋是非常不同的，在最接近的同源蚊子OBPs。本研究为设计小分子抑制剂防治蝗虫提供了结构基础。
Locusta migratoria(Lmig) causes enormous losses to agricultural products, especially because it often infests the world with great swarms as locust plagues. Locusts find their plant hosts on which they feed through their olfactory system, in which odorant binding proteins (OBPs) play an important role. Previous study indicated that the amino acid sequences of LmigOBP showed low similarity to OBPs from other insect orders and we speculated that it might perform unique binding behavior. Here, we solved the first LmigOBP1 structure at 1.65 Å, which is a monomer in solution and disulfide bonds play a key role in maintaining its function. We show that LmigOBP1 possesses a unique seventh α-helix, which is located at the surface with strong interactions with the LmigOBP1 scaffold consisting of other six α-helices. Moreover, the seventh α-helix forms a wall of an “L” shaped internal hydrophobic cavity to accommodate linear ligands, which is consistent with the binding experiments. We also demonstrate that the ligand-binding pocket in LmigOBP1 is greatly different from that in the closest homologs mosquito OBPs. Taken together, this study provides a structural basis for designing small inhibitors to control locust.