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Crystal structures and binding dynamics of odorant-binding protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri

DOI: 10.1038/srep24739 DOI Help

Authors: Tom Northey (Birkbeck, University of London; University College London) , Herbert Venthur (Rothamsted Research; Universidad de La Frontera) , Filomena De Biasio (Rothamsted Research; Università della Basilicata) , Francois Xavier Chauviac (Birkbeck, University of London) , Ambrose Cole (Birkbeck, University of London) , Karlos Antonio Lisboa Ribeiro (Rothamsted Research) , Gerarda Grossi (Università della Basilicata) , Patrizia Falabella (Università della Basilicata) , Linda M. Field (Rothamsted Research) , Nicholas H. Keep (Birkbeck, University of London) , Jing-Jiang Zhou (Rothamsted Research)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Scientific Reports , VOL 6

State: Published (Approved)
Published: April 2016
Diamond Proposal Number(s): 7197

Open Access Open Access

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 an 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.

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography

Added On: 17/11/2016 13:11


Discipline Tags:

Biochemistry Agriculture & Fisheries Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)