4YVO

Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)

4YVO の概要

• エントリーDOI: 10.2210/pdb4yvo/pdb
• 関連するPDBエントリー: 4YVQ
• 分子名称: Protein FLUORESCENT IN BLUE LIGHT, chloroplastic (2 entities in total)
• 機能のキーワード: tpr, chloroplast, fluorescent protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Plastid, chloroplast membrane; Single-pass membrane protein: Q940U6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18425.98

構造登録者

Zhang, M.,Zhang, F.,Liu, L. (登録日: 2015-03-20, 公開日: 2015-06-10, 最終更新日: 2023-11-08)

主引用文献

Zhang, M.,Zhang, F.,Fang, Y.,Chen, X.,Chen, Y.,Zhang, W.,Dai, H.E.,Lin, R.,Liu, L.
The Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase.
J.Biol.Chem., 290:17559-17565, 2015

PubMed Abstract: The tetratricopeptide repeat (TPR)-containing protein FLU is a negative regulator of chlorophyll biosynthesis in plants. It directly interacts through its TPR domain with glutamyl-tRNA reductase (GluTR), the rate-limiting enzyme in the formation of δ-aminolevulinic acid (ALA). Delineation of how FLU binds to GluTR is important for understanding the molecular basis for FLU-mediated repression of synthesis of ALA, the universal tetrapyrrole precursor. Here, we characterize the FLU-GluTR interaction by solving the crystal structures of the uncomplexed TPR domain of FLU (FLU(TPR)) at 1.45-Å resolution and the complex of the dimeric domain of GluTR bound to FLU(TPR) at 2.4-Å resolution. Three non-canonical TPR motifs of each FLU(TPR) form a concave surface and clamp the helix bundle in the C-terminal dimeric domain of GluTR. We demonstrate that a 2:2 FLU(TPR)-GluTR complex is the functional unit for FLU-mediated GluTR regulation and suggest that the formation of the FLU-GluTR complex prevents glutamyl-tRNA, the GluTR substrate, from binding with this enzyme. These results also provide insights into the spatial regulation of ALA synthesis by the membrane-located FLU protein.

PubMed: 26037924
DOI: 10.1074/jbc.M115.662981

実験手法

X-RAY DIFFRACTION (1.45 Å)