6JPM
Crystal Structure of Odorant Binding Protein 4 in the Natural Predator Chrysopa pallens
6JPM の概要
| エントリーDOI | 10.2210/pdb6jpm/pdb |
| 分子名称 | Odorant binding protein 4 (2 entities in total) |
| 機能のキーワード | chrysopa pallens (rambur), odorant binding protein 4, structural protein |
| 由来する生物種 | Chrysopa pallens (Green lacewing) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 27466.13 |
| 構造登録者 | |
| 主引用文献 | Li, T.T.,Liu, W.C.,Zhu, J.,Yang, Y.H.,Ma, C.,Lu, C.,Zhang, K.X. Crystal structure and ligand identification of odorant binding protein 4 in the natural predator Chrysopa pallens. Int.J.Biol.Macromol., 141:1004-1012, 2019 Cited by PubMed Abstract: Green lacewing Chrysopa pallens (Rambur) is a general predator of many agricultural pests and plays a pivotal role in reducing crop damage by managing insect pest populations. Odorant binding proteins (OBPs) in insects can sense the semiochemicals in the environment and initiate the delivery of signals to their receptors. However, no Chrysopa pallens OBP (CpalOBP) structure has been reported yet, and their corresponding candidate semiochemicals are still largely unknown. Here, we reported the structure of CpalOBP4 solved with X-ray diffraction and showed its potential ligands. Our results showed that CpalOBP4 has a classical OBP structure with six α-helices and three disulfide bridges, and it can bind with farnesene, 2-tridecanone, cis-3-hexenyl hexanoate, nerolidol and farnesol through a central hydrophobic cavity. Our molecular docking results showed that Met31, Met78, Leu98, Phe141, Leu142 and Pro143 in the hydrophobic cavity were the key residues mediating the interaction of CpalOBP4 with farnesene, 2-tridecanone and cis-3-hexenyl hexanoate, which was further proven by the results that mutations of these residues led to significantly reduced binding affinities of CpalOBP4 for these ligands. Our study provides useful information for the further investigation of the biological function of CpalOBP4 as well as important cues for improving biological control in agriculture. PubMed: 31525411DOI: 10.1016/j.ijbiomac.2019.09.043 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.098 Å) |
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