6LYW
Structural insight into the biological functions of Arabidopsis thaliana ACHT1
Summary for 6LYW
| Entry DOI | 10.2210/pdb6lyw/pdb |
| Descriptor | Thioredoxin-like 2-1, chloroplastic, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | arabidopsis thaliana, 2-cys prxa, peroxidase activity., structural protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 35113.98 |
| 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 citation | 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 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: 32376247DOI: 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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