Crystallization (Comment) | Organism |
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three purified electron transfer complexes of FTR and Trx isoforms. Crystals of FTR:Trx-y1, FTR:Trx-f2, and FTR:Trx-m2 are obtained by the hanging drop vapor diffusion method. Crystals of FTR:Trx-y1 are obtained from droplets comprising 0.001 ml of 10 mg/ml protein solution and 0.001 ml of reservoir solution containing 100 mM magnesium citric acid, pH 3.5, 5% v/v 2-propanol, and 5-9% w/v PEG 3350, at 20°C. Crystals of FTR:Trx-f2 are obtained from droplets comprising 0.001 ml of 10 mg/ml protein solution and 0.001 ml of reservoir solution containing 200 mM magnesium nitrate and 16-20% w/v PEG 3350, at 20°C. Crystals of FTR:Trx-m2 are obtained from droplets comprising 0.001 ml of 10 mg/ml protein solution and 0.001 ml of reservoir solution containing 100 mM sodium citrate, pH 6.2, and 18% w/v PEG 3350, at 4°C. Crystals of Trx-m1 are obtained by sitting-drop vapor diffusion method from droplets comprising 200 nl of 10 mg/ml protein solution and 200 nl of reservoir solution containing in 0.1 M HEPES-NaOH, pH 7.5, 10% v/v 2-propanol, and 20% w/v PEG 4000, at 20°C. X-ray diffraction structure determination analysis. The crystal structure of FTR:Trx-y1 is solved using the molecular replacement method at 1.59 A resolution without any ambiguity. The structure of the FTR:Trx-f2 complex is determined at 1.8 A resolution by molecular replacement using Synechosystis FTR and spinach Trx-f structure (PDB ID 2PU9) as a search model. Crystals of the FTR:Trx-m2 complex comprise 7 complexes in the asymmetric unit with a high solvent content of 71.9%, giving a resolution of 2.4 A. Structure modeling | Arabidopsis thaliana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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chloroplast | - |
Arabidopsis thaliana | 9507 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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2 reduced ferredoxin + thioredoxin disulfide | Arabidopsis thaliana | - |
2 oxidized ferredoxin + thioredoxin + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
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Arabidopsis thaliana | Q9SJ89 | - |
- |
Source Tissue | Comment | Organism | Textmining |
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leaf | - |
Arabidopsis thaliana | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin + thioredoxin disulfide | - |
Arabidopsis thaliana | 2 oxidized ferredoxin + thioredoxin + 2 H+ | - |
? | |
additional information | 10 thioredoxin (Trx) isoforms in Arabidopsis thaliana can be clustered into three classes based on the kinetics of the ferredoxin-thioredoxin reductase (FTR)-dependent reduction (high-, middle-, and low-efficiency classes). Analysis of interaction between FTR and Trxs in the complex, structure analyses, detailed overview | Arabidopsis thaliana | ? | - |
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Synonyms | Comment | Organism |
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Fd-thioredoxin reductase | - |
Arabidopsis thaliana |
ferredoxin-thioredoxin reductase | - |
Arabidopsis thaliana |
FTR | - |
Arabidopsis thaliana |
Cofactor | Comment | Organism | Structure |
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Ferredoxin | - |
Arabidopsis thaliana |
General Information | Comment | Organism |
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metabolism | thiol-based redox regulation is a mechanism for controlling metabolic pathways in chloroplasts. Thioredoxin (Trx) possesses a pair of redox-active cysteines that activates specific enzymes in a light-dependent manner. The redox level of Trx is maintained by ferredoxin-Trx reductase (FTR) and ferredoxin (Fd), the latter being the final electron acceptor in the photosynthetic electron transport chain. In this Fd/Trx cascade, electrons are sequentially transmitted from photosystem I, via Fd, FTR, and Trx, to target enzymes such as fructose-1,6-bisphosphatase, sedoheptulose-bisphosphatase, NADP-malate dehydrogenase, or 2-Cys peroxiredoxins | Arabidopsis thaliana |
additional information | superposition of the FTR structure with/without Trx showed no main chain structural changes upon complex formation. There is 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 shows 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 | Arabidopsis thaliana |
physiological function | 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 | Arabidopsis thaliana |