7C3F
Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex
Summary for 7C3F
| Entry DOI | 10.2210/pdb7c3f/pdb |
| Descriptor | Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic, Ferredoxin-thioredoxin reductase variable chain, chloroplastic, Thioredoxin M2, chloroplastic, ... (6 entities in total) |
| Functional Keywords | ftr, trx m2, electron transport |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Total number of polymer chains | 23 |
| Total formula weight | 294855.39 |
| Authors | Kurisu, G.,Juniar, L.,Tanaka, H. (deposition date: 2020-05-12, release date: 2020-10-14, Last modification date: 2024-11-06) |
| Primary citation | Juniar, L.,Tanaka, H.,Yoshida, K.,Hisabori, T.,Kurisu, G. Structural basis for thioredoxin isoform-based fine-tuning of ferredoxin-thioredoxin reductase activity. Protein Sci., 29:2538-2545, 2020 Cited by PubMed Abstract: Photosynthetic electron transport occurs on the thylakoid membrane of chloroplasts. Ferredoxin (Fd), the final acceptor in the electron transport chain, distributes electrons to several Fd-dependent enzymes including Fd-thioredoxin reductase (FTR). A cascade from Fd to FTR further reduces Thioredoxin (Trx), which tunes the activity of target metabolic enzymes eventually in a light-dependent manner. We previously reported that 10 Trx isoforms in Arabidopsis thaliana can be clustered into three classes based on the kinetics of the FTR-dependent reduction (high-, middle-, and low-efficiency classes). In this study, we determined the X-ray structure of three electron transfer complexes of FTR and Trx isoform, Trx-y1, Trx-f2, and Trx-m2, as representative examples of each class. Superposition of the FTR structure with/without Trx showed no main chain structural changes upon complex formation. There was no significant conformational change for single and complexed Trx-m structures. Nonetheless, the interface of FTR:Trx complexes displayed significant variation. Comparative analysis of the three structures showed two types of intermolecular interactions; (i) common interactions shared by all three complexes and (ii) isoform-specific interactions, which might be important for fine-tuning FTR:Trx activity. Differential electrostatic potentials of Trx isoforms may be key to isoform-specific interactions. PubMed: 33015914DOI: 10.1002/pro.3964 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3986 Å) |
Structure validation
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