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  • 1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein from the agricultural pest Ostrinia furnacalis (OfurPBP2)
Title: 1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein from the agricultural pest Ostrinia furnacalis (OfurPBP2)
Ostrinia furnacalis, a lepidopteran moth, is an invasive pest found in Asia, Australia, Africa and parts of the United States. The Ostrinia 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.  more » « less
Award ID(s):
1807722
PAR ID:
10159529
Author(s) / Creator(s):
Date Published:
Journal Name:
Biomolecular NMR assignments
ISSN:
1874-2718
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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