NMR chemical shift assignment of Drosophila odorant binding protein 44a in complex with 8(Z)-eicosenoic acid

• DOI: 10.1007/s12104-024-10178-2
• Publication Date: 2024-06-01T05:01:35Z
• Authors: Myriam L. Cotten; Mary R. Starich; Yi He; Jun Yin; Quan Yuan; Nico Tjandra
• Keywords: Fatty Acids, Monounsaturated; 0301 basic medicine; 03 medical and health sciences; Drosophila melanogaster; Animals; Drosophila Proteins; Amino Acid Sequence; Receptors, Odorant; Nuclear Magnetic Resonance, Biomolecular; Article; Protein Binding

Abstract The odorant binding protein, OBP44a is one of the most abundant proteins expressed in brain developing fruit fly Drosophila melanogaster . Its cellular function has not yet been determined. OBP family well established to recognize hydrophobic molecules. In this study, NMR employed structurally characterize OBP44a. chemical shift perturbation measurements confirm that binds fatty acids. Complete assignments backbone shifts and secondary analysis demonstrate apo state comprised six α-helices. Upon 8(Z)-eicosenoic acid (8(Z)-C20:1), C-terminal region undergoes a conformational change, from unstructured α-helical. addition restructuring upon ligand binding, some residues show dramatic changes. Surprisingly, several charged are also strongly affected by lipid binding. Some these could represent key structural features relies on perform its function. assignment first step towards characterizing structure how specific might play role release. This information will be important deciphering biological during development.