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Abstract
In potato (Solanum tuberosum L.), 14-3-3 protein forms a protein complex with the FLOWERING LOCUS T (FT)-like protein StSP6A and the FD-like protein StFDL1 to activate potato tuber formation. Eleven 14-3-3 isoforms were reported in potato, designated as St14a-k. In this study, the crystal structure of the free form of St14f was determined at 2.5 Å resolution. Three chains were included in the asymmetric unit of the St14f free form crystal, and the structural deviation among the three chain structures was found on the C-terminal helix H and I. The St14f free form structure in solution was also investigated by nuclear magnetic resonance (NMR) residual dipolar coupling analysis, and the chain B in the crystal structure was consistent with NMR data. Compared to other crystal structures, St14f helix I exhibited a different conformation with larger B-factor values. Larger B-factor values on helix I were also found in the 14-3-3 free form structure with higher solvent contents. The mutation in St14f Helix I stabilized the complex with StFDL1. These data clearly showed that the flexibility of helix I of 14-3-3 protein plays an important role in the recognition of target protein.
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Details
1 Osaka University, Institute for Protein Research, Suita, Japan (GRID:grid.136593.b) (ISNI:0000 0004 0373 3971)
2 Yokohama City University, Kihara Institute for Biological Research, Yokohama, Japan (GRID:grid.268441.d) (ISNI:0000 0001 1033 6139)
3 Osaka University, Institute for Protein Research, Suita, Japan (GRID:grid.136593.b) (ISNI:0000 0004 0373 3971); Yokohama National University, Graduate School of Engineering Science, Yokohama, Japan (GRID:grid.268446.a) (ISNI:0000 0001 2185 8709)