5YJL

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with NADPH and GBP

5YJL の概要

• エントリーDOI: 10.2210/pdb5yjl/pdb
• 分子名称: Glutamyl-tRNA reductase 1, Glutamyl-tRNA reductase-binding protein, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: gtr, ala, tetrapyrrole, photosynthesis
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 174311.91

構造登録者

Zhao, A.,Han, F. (登録日: 2017-10-11, 公開日: 2018-05-30, 最終更新日: 2023-11-22)

主引用文献

Zhao, A.,Han, F.
Crystal structure of Arabidopsis thaliana glutamyl-tRNAGlureductase in complex with NADPH and glutamyl-tRNAGlureductase binding protein
Photosyn. Res., 137:443-452, 2018

PubMed Abstract: In higher plants, the tetrapyrrole biosynthesis pathway starts from the reaction catalyzed by the rate-limiting enzyme, glutamyl-tRNA reductase (GTR). In Arabidopsis thaliana, GTR is controlled by post-transcriptional regulators such as GTR binding protein (GBP), which stimulates AtGTR activity. The NADPH-binding domain of AtGTR undergoes a substantial movement upon GBP binding. Here, we report the crystal structure of AtGTR-NADPH-GBP ternary complex. NADPH binding causes slight structural changes compared with the AtGTR-GBP binary complex, and possibly take a part of the space needed by the substrate glutamyl-tRNA. The highly reactive sulfhydryl group of the active-site residue Cys144 shows an obvious rotation, which may facilitate the hydride transfer from NADPH to the thioester intermediate to form glutamate-1-semialdehyde. Furthermore, Lys271, Lys274, Ser275, Asn278, and Gln282 of GBP participate in the interaction between AtGTR and GBP, and the stimulating effect of GBP decreased when all of these residues were mutated to Ala. When the Cys144 of AtGTR was mutated to Ser, AtGTR activity could not be detected even in the presence of GBP.

PubMed: 29785497
DOI: 10.1007/s11120-018-0518-8

実験手法

X-RAY DIFFRACTION (2.7 Å)