6LYW

Structural insight into the biological functions of Arabidopsis thaliana ACHT1

6LYW の概要

• エントリーDOI: 10.2210/pdb6lyw/pdb
• 分子名称: Thioredoxin-like 2-1, chloroplastic, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: arabidopsis thaliana, 2-cys prxa, peroxidase activity., structural protein
• 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: 35113.98

構造登録者

Wang, J.C.,Pan, W.M.,Wang, M.Z.,Zhang, M. (登録日: 2020-02-16, 公開日: 2020-05-13, 最終更新日: 2024-10-09)

主引用文献

Wang, J.,Pan, W.,Cai, W.,Wang, M.,Liu, L.,Zhang, M.
Structural insight into the biological functions of Arabidopsis thaliana ACHT1.
Int.J.Biol.Macromol., 158:43-51, 2020

PubMed Abstract: The Arabidopsis thaliana atypical Cys His-rich thioredoxins (ACHTs) are a small class of atypical thioredoxins (TRXs) located in chloroplasts thylakoids and are characterized by a noncanonical motif at their redox active site, C (G/S)(S/G)C. Previous studies have reported that ACHT1 can interact with A. thaliana 2-Cys peroxiredoxins (2-Cys Prxs, including PrxA and PrxB) to transmit oxidation signals in response to illumination with normal light intensity. In this study, we reported the crystal structure of ACHT1 and show that ACHT1 adopts a canonical TRX fold. Comparison of the structures of ACHT1 in both reducing and oxidizing environments revealed that while the redox environment did not influence the overall structure of ACHT1, it did change the conformation of its catalytic residues. We found that the catalytic C125 of ACHT1 is the target residue for PrxA in vitro. In addition, we found that ACHT1 can reduce the peroxidase activity of PrxA, and further confirmed that the ability of ACHT1 to restore the peroxidase function of PrxA was due to the interaction between the two. Our results provide a structural basis for studying the function of atypical TRXs and the oxidative regulation mechanism of ACHT1 and 2-Cys Prxs in chloroplasts.

PubMed: 32376247
DOI: 10.1016/j.ijbiomac.2020.04.246

実験手法

X-RAY DIFFRACTION (1.7 Å)