Author:
Harada Ken-ichi,Furuita Kyoko,Yamashita Eiki,Taoka Ken-ichiro,Tsuji Hiroyuki,Fujiwara Toshimichi,Nakagawa Atsushi,Kojima Chojiro
Abstract
AbstractIn 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.
Funder
Japan Synchrotron Radiation Research Institute
Japan Agency for Medical Research and Development
Ministry of Education, Culture, Sports, Science and Technology
Japan Science and Technology Agency
Institute for Protein Research, Osaka University
Publisher
Springer Science and Business Media LLC
Cited by
1 articles.
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