6IGG

Crystal structure of FT condition 1

Summary for 6IGG

• Entry DOI: 10.2210/pdb6igg/pdb
• Descriptor: Protein FLOWERING LOCUS T, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: flowering control, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 19930.44

Authors

Watanabe, S.,Nakamura, Y.,Kanehara, K.,Inaba, K. (deposition date: 2018-09-25, release date: 2019-12-25, Last modification date: 2023-11-22)

Primary citation

Nakamura, Y.,Lin, Y.C.,Watanabe, S.,Liu, Y.C.,Katsuyama, K.,Kanehara, K.,Inaba, K.
High-Resolution Crystal Structure of Arabidopsis FLOWERING LOCUS T Illuminates Its Phospholipid-Binding Site in Flowering.
Iscience, 21:577-586, 2019

PubMed Abstract: Arabidopsis FLOWERING LOCUS T (FT) is a pivotal component of florigen, a long-range mobile flowering signal. Here, we determined the 1.0 Å-resolution crystal structure of FT, a significantly higher-resolution crystal structure of FT than previously reported one (2.6 Å). 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 (PC), 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 PC binding in modulating FT function. Our structural, biochemical, and transgenic analyses reveal the molecular mechanism of PC binding in FT-mediated flowering time control.

PubMed: 31726375
DOI: 10.1016/j.isci.2019.10.045

Experimental method

X-RAY DIFFRACTION (1 Å)