7uo6 | pdb_00007uo6

NMR structure of Pheromone-binding protein 2 in Ostrinia furnacalis

spinqualitylabelsall models 7uo6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7uo6 is a 1 chain structure with sequence from Ostrinia furnacalis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E7CCA0_OSTFU Publication Abstract from PubMed Ostrinia furnacalis is an invasive lepidopteran agricultural pest that relies on olfaction for mating and reproduction. Male moths have an extremely sensitive olfactory system that can detect the sex pheromones emitted by females over a great distance. Pheromone-binding proteins present in the male moth antenna play a key role in the pheromone uptake, transport, and release at the dendritic membrane of the olfactory neuron. Here, we report the first high-resolution NMR structure of a pheromone-binding protein from an Ostrinia species at pH 6.5. The core of the Ostrinia furnacalis PBP2 (OfurPBP2) consists of six helices, alpha1a (2-14), alpha1b (16-22), alpha2 (27-37), alpha3 (46-60), alpha4 (70-80), alpha5 (84-100), and alpha6 (107-124) surrounding a large hydrophobic pocket. The structure is stabilized by three disulfide bridges, 19-54, 50-108, and 97-117. In contrast to the unstructured C-terminus of other lepidopteran PBPs, the C-terminus of OfurPBP2 folds into an alpha-helix (alpha7) at pH 6.5. The protein has nanomolar affinity towards both pheromone isomers. Molecular docking of both pheromones, E-12 and Z-12-tetradecenyl acetate, to OfurPBP2 revealed that the residues Met5, Lys6, Met8, Thr9, Phe12, Phe36, Trp37, Phe76, Ser115, Phe118, Lys119, Ile122, His123, and Ala128 interact with both isomers, while Thr9 formed a hydrogen bond with the acetate head group. NMR structure and thermal unfolding studies with CD suggest that ligand release at pH 4.5 is likely due to the partial unfolding of the protein. Ostrinia furnacalis PBP2 solution NMR structure: Insight into ligand binding and release mechanisms.,Dahal SR, Lewellen JL, Ayyappan S, Chaudhary BP, Nukala V, Mohanty S Protein Sci. 2022 Oct;31(10):e4438. doi: 10.1002/pro.4438. PMID:36173163 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pheromone binding protein

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