5CHE

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins

5CHE の概要

• エントリーDOI: 10.2210/pdb5che/pdb
• 分子名称: Glutamyl-tRNA reductase 1, chloroplastic, Glutamyl-tRNA reductase-binding protein, chloroplastic, Protein FLUORESCENT IN BLUE LIGHT, chloroplastic, ... (4 entities in total)
• 機能のキーワード: glutr, tertiary complex, regulatory proteins, anchor protein, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• 細胞内の位置: Plastid, chloroplast membrane : P42804; Plastid, chloroplast stroma : Q9LU39; Plastid, chloroplast membrane ; Single-pass membrane protein: Q940U6
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 208367.63

構造登録者

Fang, Y.,Liu, L. (登録日: 2015-07-10, 公開日: 2016-02-03, 最終更新日: 2023-11-08)

主引用文献

Fang, Y.,Zhao, S.,Zhang, F.,Zhao, A.,Zhang, W.,Zhang, M.,Liu, L.
The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein
Sci Rep, 6:19756-19756, 2016

PubMed Abstract: Tetrapyrrole biosynthesis is an essential and tightly regulated process, and glutamyl-tRNA reductase (GluTR) is a key target for multiple regulatory factors at the post-translational level. By binding to the thylakoid membrane protein FLUORESCENT (FLU) or the soluble stromal GluTR-binding protein (GBP), the activity of GluTR is down- or up-regulated. Here, we reconstructed a ternary complex composed of the C-terminal tetratricopepetide-repeat domain of FLU, GBP, and GluTR, crystallized and solved the structure of the complex at 3.2 Å. The overall structure resembles the shape of merged two binary complexes as previously reported, and shows a large conformational change within GluTR. We also demonstrated that GluTR binds tightly with GBP but does not bind to GSAM under the same condition. These findings allow us to suggest a biological role of the ternary complex for the regulation of plant GluTR.

PubMed: 26794057
DOI: 10.1038/srep19756

実験手法

X-RAY DIFFRACTION (3.203 Å)