Abstract
Ostrinia furnacalis, a lepidopteran moth, is an invasive pest found in Asia, Australia, Africa, and parts of the United States. The O. furnacalis pheromone-binding protein2 (OfurPBP2), present in the male moth antenna, plays a role in the detection of female-secreted pheromone in a process that leads to mating. To understand the structural mechanism of pheromone binding and release in this pest, we have initiated characterization of OfurPBP2 by solution NMR. Here, we report the backbone resonance assignments and the secondary structural elements of OfurPBP2 at pH 6.5 using uniformly 13C, 15N-labeled protein with various triple resonance NMR experiments. The assignments are 97% completed for backbone and 88% completed for side-chain resonances. The secondary structure of OfurPBP2, based on backbone chemical shifts, consists of eight α-helices, including a well-structured C-terminal helix.
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Acknowledgements
This research was financially supported by National Science Foundation Award CHE-1807722 to Smita Mohanty. We thank Dr. David Zoetewey for numerous useful discussions. All NMR data were collected at the National High Magnetic Field Laboratory, which is supported by National Science Foundation Cooperative Agreement No. DMR-1644779 and the State of Florida. We thank Dr. Thomas Webb of Auburn University for the critical reading of this manuscript.
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SM conceived, designed the strategies and techniques employed, supervised the research, and analyzed the data. SD and BC conducted NMR experiments. SD and JL processed and analyzed NMR data and completed the NMR resonance assignments. SM and SD wrote the paper and SD and JL prepared figures.
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Dahal, S.R., Lewellen, J.L., Chaudhary, B.P. et al. 1H, 13C, and 15N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2). Biomol NMR Assign 14, 115–118 (2020). https://doi.org/10.1007/s12104-020-09930-1
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DOI: https://doi.org/10.1007/s12104-020-09930-1