7XBQ

Crystal structure of potato 14-3-3 protein St14f

Summary for 7XBQ

• Entry DOI: 10.2210/pdb7xbq/pdb
• Descriptor: Putative 14-3-3 protein (1 entity in total)
• Functional Keywords: plant protein
• Biological source: Solanum tuberosum (potato)
• Total number of polymer chains: 3
• Total formula weight: 87734.11

Authors

Harada, K.,Kojima, C.,Yamashita, E.,Nakagawa, A. (deposition date: 2022-03-21, release date: 2022-07-20, Last modification date: 2023-11-29)

Primary citation

Harada, K.I.,Furuita, K.,Yamashita, E.,Taoka, K.I.,Tsuji, H.,Fujiwara, T.,Nakagawa, A.,Kojima, C.
Crystal structure of potato 14-3-3 protein St14f revealed the importance of helix I in StFDL1 recognition.
Sci Rep, 12:11596-11596, 2022

PubMed 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.

PubMed: 35804047
DOI: 10.1038/s41598-022-15505-y

Experimental method

X-RAY DIFFRACTION (2.45 Å)