High-resolution crystal structure of Arabidopsis FLOWERING LOCUS T illuminates its phospholipid-binding site in flowering: Structural basis for phospholipid binding to FT

Summary Arabidopsis FLOWERING LOCUS T (FT) is a pivotal component of florigen, a long-range mobile flowering signal. Here, we determined the 1.0 A-resolution crystal structure of FT, a significantly higher-resolution crystal structure of FT than previously reported one (2.6 A). The present crystallographic studies revealed 4 alternative configurations with the precise location of the surrounding water molecules. Using this structural data, computational docking simulation predicted the putative binding sites for phosphatidylcholine, an endogenous ligand that interacts with FT to modulate flowering time. In vitro reconstitution of the lipid–protein interaction showed that mutations at two of the predicted sites significantly compromised the lipid binding ability of FT. In planta, one of the mutant FT proteins significantly affected FT function in flowering, emphasizing the involvement of phosphatidylcholine binding in modulating FT function. Our structural, biochemical and transgenic analyses reveal the molecular mechanism of phosphatidylcholine binding in FT–mediated flowering time control.