5ECQ

Crystal Structure of FIN219-FIP1 complex with JA, VAL and ATP

5ECQ の概要

• エントリーDOI: 10.2210/pdb5ecq/pdb
• 関連するPDBエントリー: 5ECH 5ECI 5ECK 5ECL 5ECM 5ECN 5ECO 5ECP 5ECR 5ECS
• 分子名称: Jasmonic acid-amido synthetase JAR1, Glutathione S-transferase U20, {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid, ... (7 entities in total)
• 機能のキーワード: jasmonate-amido synthetase, glutathione s-transferase, ligase-transferase complex, ligase/transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• 細胞内の位置: Cytoplasm : Q9SKE2; Nucleus : Q8L7C9
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 235200.13

構造登録者

Chen, C.Y.,Cheng, Y.S. (登録日: 2015-10-20, 公開日: 2016-11-02, 最終更新日: 2023-11-08)

主引用文献

Chen, C.Y.,Ho, S.S.,Kuo, T.Y.,Hsieh, H.L.,Cheng, Y.S.
Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation
Proc. Natl. Acad. Sci. U.S.A., 114:E1815-E1824, 2017

PubMed Abstract: Far-red (FR) light-coupled jasmonate (JA) signaling is necessary for plant defense and development. FR insensitive 219 (FIN219) is a member of the Gretchen Hagen 3 (GH3) family of proteins in and belongs to the adenylate-forming family of enzymes. It directly controls biosynthesis of jasmonoyl-isoleucine in JA-mediated defense responses and interacts with FIN219-interacting protein 1 (FIP1) under FR light conditions. FIN219 and FIP1 are involved in FR light signaling and are regulators of the interplay between light and JA signaling. However, how their interactions affect plant physiological functions remains unclear. Here, we demonstrate the crystal structures of FIN219-FIP1 while binding with substrates at atomic resolution. Our results show an unexpected FIN219 conformation and demonstrate various differences between this protein and other members of the GH3 family. We show that the rotated C-terminal domain of FIN219 alters ATP binding and the core structure of the active site. We further demonstrate that this unique FIN219-FIP1 structure is crucial for increasing FIN219 activity and determines the priority of substrate binding. We suggest that the increased FIN219 activity resulting from the complex form, a conformation for domain switching, allows FIN219 to switch to its high-affinity mode and thereby enhances JA signaling under continuous FR light conditions.

PubMed: 28223489
DOI: 10.1073/pnas.1609980114

実験手法

X-RAY DIFFRACTION (1.66 Å)