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6LYW

Structural insight into the biological functions of Arabidopsis thaliana ACHT1

Summary for 6LYW
Entry DOI10.2210/pdb6lyw/pdb
DescriptorThioredoxin-like 2-1, chloroplastic, GLYCEROL, SULFATE ION, ... (4 entities in total)
Functional Keywordsarabidopsis thaliana, 2-cys prxa, peroxidase activity., structural protein
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Total number of polymer chains2
Total formula weight35113.98
Authors
Wang, J.C.,Pan, W.M.,Wang, M.Z.,Zhang, M. (deposition date: 2020-02-16, release date: 2020-05-13, Last modification date: 2024-10-09)
Primary citationWang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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数据于2025-12-03公开中

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