Reveals conformational change and pH dependence of fatty acid binding in the odorant-binding protein OBP44a from Drosophila, highlighting its role in cellular signaling.
Key Points
This research aims to determine the structure of OBP44a and characterize its fatty acid binding at variable pH levels.
NMR structure determination of OBP44a bound to eicosenoic acid.
Fatty acid-binding assays conducted at different pH levels.
Identification of residues sensitive to pH and involvement in ligand release.
OBP44a undergoes a conformational change upon fatty acid binding.
Formation of a 7th alpha-helix was observed relative to the apo state.
The apo form of OBP44a appears at lower pH, suggesting an allosteric mechanism.