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    Crystal structures and binding dynamics of Odorant-Binding Protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri

    Northey, Thomas and Venthur, H. and De Biasio, F. and Chauviac, Francois-Xavier and Cole, Ambrose and Lisboa Ribeiro Junior, K.A. and Grossi, G. and Falabella, P. and Field, L.M. and Keep, Nicholas H. and Zhou, J.J. (2016) Crystal structures and binding dynamics of Odorant-Binding Protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri. Scientific Reports 6 , p. 24739. ISSN 2045-2322.

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    Abstract

    Aphids use chemical cues to locate hosts and find mates. The vetch aphid Megoura viciae feeds exclusively on the Fabaceae, whereas the currant-lettuce aphid Nasonovia ribisnigri alternates hosts between the Grossulariaceae and Asteraceae. Both species use alarm pheromones to warn of dangers. For N. ribisnigri this pheromone is a single component (E)-β-farnesene but M. viciae uses a mixture of (E)-β-farnesene, (-)-α- pinene, β-pinene, and limonene. Odorant-binding proteins (OBP) are believed to capture and transport such semiochemicals to their receptors. Here, we report the first aphid OBP crystal structures and examine their molecular interactions with the alarm pheromone components. Our study reveals some unique structural features: 1) the lack of internal ligand binding site; 2) a striking groove in the surface of the proteins as a putative binding site; 3) the N-terminus rather than the C-terminus occupies the site closing off the conventional OBP pocket. The results from fluorescent binding assays, molecular docking and dynamics demonstrate that OBP3 from M. viciae can bind to all four alarm pheromone components and the differential ligand binding between these very similar OBP3s from the two aphid species is determined mainly by the direct π-π interactions between ligands and the aromatic residues of OBP3s in the binding pocket.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): odorant-binding protein, aphid, (E)-ß-farnesene, crystal structure, molecular docking, repellent, binding pocket
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Nick Keep
    Date Deposited: 22 Apr 2016 12:34
    Last Modified: 02 Aug 2023 17:23
    URI: https://eprints.bbk.ac.uk/id/eprint/14853

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