1KMH

Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin

1KMH の概要

• エントリーDOI: 10.2210/pdb1kmh/pdb
• 関連するPDBエントリー: 1FX0
• 分子名称: ATPase alpha subunit, ATPase beta subunit, TENTOXIN (3 entities in total)
• 機能のキーワード: protein-inhibitor complex, hydrolase
• 由来する生物種: Spinacia oleracea (spinach); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109841.27

構造登録者

Groth, G. (登録日: 2001-12-16, 公開日: 2002-03-13, 最終更新日: 2024-12-25)

主引用文献

Groth, G.
Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin.
Proc.Natl.Acad.Sci.USA, 99:3464-3468, 2002

PubMed Abstract: Tentoxin, a natural cyclic tetrapeptide produced by phytopathogenic fungi from the Alternaria species affects the catalytic function of the chloroplast F(1)-ATPase in certain sensitive species of plants. In this study, we show that the uncompetitive inhibitor tentoxin binds to the alphabeta-interface of the chloroplast F(1)-ATPase in a cleft localized at betaAsp-83. Most of the binding site is located on the noncatalytic alpha-subunit. The crystal structure of the tentoxin-inhibited CF(1)-complex suggests that the inhibitor is hydrogen bonded to Asp-83 in the catalytic beta-subunit but forms hydrophobic contacts with residues Ile-63, Leu-65, Val-75, Tyr-237, Leu-238, and Met-274 in the adjacent alpha-subunit. Except for minor changes around the tentoxin-binding site, the structure of the chloroplast alpha(3)beta(3)-core complex is the same as that determined with the native chloroplast ATPase. Tentoxin seems to act by inhibiting inter-subunit contacts at the alphabeta-interface and by blocking the interconversion of binding sites in the catalytic mechanism.

PubMed: 11904410
DOI: 10.1073/pnas.052546099

実験手法

X-RAY DIFFRACTION (3.4 Å)