title: Crystal structure of the Locusta migratoria odorant binding protein.
abstract: 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 1.65Å, 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.
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Jiangge
authors.initials: J
authors.lastname: Zheng
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Junru
authors.initials: J
authors.lastname: Li
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China; Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center of Cancer, Tianjin 300060, China.
authors.forename: Lei
authors.initials: L
authors.lastname: Han
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Yang
authors.initials: Y
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Wei
authors.initials: W
authors.lastname: Wu
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Xiaoxuan
authors.initials: X
authors.lastname: Qi
authors.affiliation: Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.
authors.forename: Ye
authors.initials: Y
authors.lastname: Tao
authors.affiliation: Department of Entomology, China Agricultural University, Beijing 100193, China.
authors.forename: Long
authors.initials: L
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Ziding
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China. Electronic address: chenzhongzhou@cau.edu.cn.
authors.forename: Zhongzhou
authors.initials: Z
authors.lastname: Chen
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry; D015195:Drug Design; D019476:Insect Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry*; D048188:Locusta migratoria / Q000378:metabolism*; D017433:Protein Structure, Secondary; D018035:Receptors, Odorant / Q000037:antagonists & inhibitors / Q000737:chemistry*
chemical_list: D019476:Insect Proteins; D018035:Receptors, Odorant; C045648:odorant-binding protein; D003545:Cysteine
keywords: Crystal structure; Ligand binding mechanism; Locusta migratoria; Odorant binding protein; Odorant perception