5A5K

AtGSTF2 from Arabidopsis thaliana in complex with camalexin

5A5K の概要

• エントリーDOI: 10.2210/pdb5a5k/pdb
• 関連するPDBエントリー: 5A4U 5A4V 5A4W
• 分子名称: GLUTATHIONE S-TRANSFERASE F2, (2Z)-2-indol-3-ylidene-3H-1,3-thiazole (3 entities in total)
• 機能のキーワード: transferase, glutathione-s-transferase, gst, plant, arabidopsis
• 由来する生物種: ARABIDOPSIS THALIANA (THALE CRESS)
• 細胞内の位置: Cytoplasm, cytosol : P46422
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 584707.82

構造登録者

Ahmad, L.,Rylott, E.,Bruce, N.C.,Edwards, R.,Grogan, G. (登録日: 2015-06-18, 公開日: 2016-06-29, 最終更新日: 2024-01-10)

主引用文献

Ahmad, L.,Rylott, E.L.,Bruce, N.C.,Edwards, R.,Grogan, G.
Structural evidence for Arabidopsis glutathione transferase AtGSTF2 functioning as a transporter of small organic ligands.
FEBS Open Bio, 7:122-132, 2017

PubMed Abstract: Glutathione transferases (GSTs) are involved in many processes in plant biochemistry, with their best characterised role being the detoxification of xenobiotics through their conjugation with glutathione. GSTs have also been implicated in noncatalytic roles, including the binding and transport of small heterocyclic ligands such as indole hormones, phytoalexins and flavonoids. Although evidence for ligand binding and transport has been obtained using gene deletions and ligand binding studies on purified GSTs, there has been no structural evidence for the binding of relevant ligands in noncatalytic sites. Here we provide evidence of noncatalytic ligand-binding sites in the phi class GST from the model plant , GSTF2, revealed by X-ray crystallography. Complexes of the GSTF2 dimer were obtained with indole-3-aldehyde, camalexin, the flavonoid quercetrin and its non-rhamnosylated analogue quercetin, at resolutions of 2.00, 2.77, 2.25 and 2.38 Å respectively. Two symmetry-equivalent-binding sites () were identified at the periphery of the dimer, and one more () at the dimer interface. In the complexes, indole-3-aldehyde and quercetrin were found at both and sites, but camalexin was found only at the sites and quercetin only at the site. Ligand binding at each site appeared to be largely determined through hydrophobic interactions. The crystallographic studies support previous conclusions made on ligand binding in noncatalytic sites by GSTF2 based on isothermal calorimetry experiments (Dixon . (2011) , 63-70) and suggest a mode of ligand binding in GSTs commensurate with a possible role in ligand transport.

PubMed: 28174680
DOI: 10.1002/2211-5463.12168

実験手法

X-RAY DIFFRACTION (2.77 Å)