6LBP

Structure of the Glutamine Phosphoribosylpyrophosphate Amidotransferase from Arabidopsis thaliana

6LBP の概要

• エントリーDOI: 10.2210/pdb6lbp/pdb
• 分子名称: Amidophosphoribosyltransferase 2, chloroplastic, IRON/SULFUR CLUSTER (2 entities in total)
• 機能のキーワード: amidotransferase, tetramer, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107388.40

構造登録者

Yi, Z.,Cao, X.,Han, F.,Feng, Y. (登録日: 2019-11-14, 公開日: 2020-04-29, 最終更新日: 2023-11-22)

主引用文献

Cao, X.,Du, B.,Han, F.,Zhou, Y.,Ren, J.,Wang, W.,Chen, Z.,Zhang, Y.
Crystal Structure of the Chloroplastic Glutamine Phosphoribosylpyrophosphate Amidotransferase GPRAT2 FromArabidopsis thaliana.
Front Plant Sci, 11:157-157, 2020

PubMed Abstract: Chloroplastic glutamine phosphoribosylpyrophosphate amidotransferase (GPRATase) catalyzes the first committed step of purine biosynthesis in , and DAS734 is a direct and specific inhibitor of AtGPRAT, with phytotoxic effects similar to the leaf beaching phenotypes of known AtGPRAT genetic mutants, especially and . However, the structure of AtGPRAT and the inhibition mode of DAS734 still remain poorly understood. In this study, we solved the structure of AtGPRAT2, which revealed structural differences between AtGPRAT2 and bacterial enzymes. Kinetics assay demonstrated that DAS734 behaves as a competitive inhibitor for the substrate phosphoribosyl pyrophosphate (PRPP) of AtGPRAT2. Docking studies showed that DAS734 forms electrostatic interactions with R264 and hydrophobic interactions with several residues, which was verified by binding assays. Collectively, our study provides important insights into the inhibition mechanism of DAS734 to AtGPRAT2 and sheds light on future studies into further development of more potent herbicides targeting GPRATases.

PubMed: 32174940
DOI: 10.3389/fpls.2020.00157

実験手法

X-RAY DIFFRACTION (3.065 Å)