1O9C

Structural view of a fungal toxin acting on a 14-3-3 regulatory complex

1O9C の概要

• エントリーDOI: 10.2210/pdb1o9c/pdb
• 関連するPDBエントリー: 1O9D 1O9E 1O9F
• 分子名称: 14-3-3-LIKE PROTEIN C, CITRATE ANION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: protein binding, fusicoccin, 14-3-3 family, activating drug, plant plasma membrane (h+)atpase
• 由来する生物種: NICOTIANA TABACUM (COMMON TOBACCO)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29624.53

構造登録者

Wurtele, M.,Jelich-Ottmann, C.,Wittinghofer, A.,Oecking, C. (登録日: 2002-12-12, 公開日: 2003-03-06, 最終更新日: 2023-12-13)

主引用文献

Wurtele, M.,Jelich-Ottmann, C.,Wittinghofer, A.,Oecking, C.
Structural View of a Fungal Toxin Acting on a 14-3-3 Regulatory Complex
Embo J., 22:987-, 2003

PubMed Abstract: The fungal phytotoxin fusicoccin stabilizes the interaction between the C-terminus of the plant plasma membrane H(+)-ATPase and 14-3-3 proteins, thus leading to permanent activation of the proton pump. This results in an irreversible opening of the stomatal pore, followed by wilting of plants. Here, we report the crystal structure of the ternary complex between a plant 14-3-3 protein, fusicoccin and a phosphopeptide derived from the C-terminus of the H(+)-ATPase. Comparison with the corresponding binary 14-3-3 complexes indicates no major conformational change induced by fusicoccin. The compound rather fills a cavity in the protein-phosphopeptide interaction surface. Isothermal titration calorimetry indicates that the toxin alone binds only weakly to 14-3-3 and that peptide and toxin mutually increase each others' binding affinity approximately 90-fold. These results are important for herbicide development but might have general implications for drug development, since rather than inhibiting protein-protein interactions, which is difficult to accomplish, it might be easier to reverse the strategy and stabilize protein-protein complexes. As the fusicoccin interaction shows, only low-affinity interactions would be required for this strategy.

PubMed: 12606564
DOI: 10.1093/EMBOJ/CDG104

実験手法

X-RAY DIFFRACTION (2.6 Å)