| Title: | "(1)H, (13)C, and (15)N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2)" |
| Author(s): | Dahal SR; Lewellen JL; Chaudhary BP; Mohanty S; |
| Address: | "Oklahoma State University Stillwater, Stillwater, OK, USA. Oklahoma State University Stillwater, Stillwater, OK, USA. smita.mohanty@okstate.edu" |
| DOI: | 10.1007/s12104-020-09930-1 |
| ISSN/ISBN: | 1874-270X (Electronic) 1874-270X (Linking) |
| 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 (13)C, (15)N-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 alpha-helices, including a well-structured C-terminal helix" |
| Keywords: | "*Agriculture Animals *Carbon-13 Magnetic Resonance Spectroscopy Carrier Proteins/*chemistry Insect Proteins/*chemistry Moths/*metabolism Nitrogen Isotopes *Nuclear Magnetic Resonance, Biomolecular Protein Structure, Secondary *Proton Magnetic Resonance Sp;" |
| Notes: | "MedlineDahal, Salik R Lewellen, Jacob L Chaudhary, Bharat P Mohanty, Smita eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Netherlands 2020/01/25 Biomol NMR Assign. 2020 Apr; 14(1):115-118. doi: 10.1007/s12104-020-09930-1. Epub 2020 Jan 23" |
