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Literature summary for 1.8.7.2 extracted from

  • Juniar, L.; Tanaka, H.; Yoshida, K.; Hisabori, T.; Kurisu, G.
    Structural basis for thioredoxin isoform-based fine-tuning of ferredoxin-thioredoxin reductase activity (2020), Protein Sci., 29, 2538-2545 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Localization Comment Organism GeneOntology No. Textmining
chloroplast
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Arabidopsis thaliana 9507
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 reduced ferredoxin + thioredoxin disulfide Arabidopsis thaliana
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2 oxidized ferredoxin + thioredoxin + 2 H+
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?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9SJ89
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-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Arabidopsis thaliana
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + thioredoxin disulfide
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Arabidopsis thaliana 2 oxidized ferredoxin + thioredoxin + 2 H+
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?
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

Synonyms Comment Organism
Fd-thioredoxin reductase
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Arabidopsis thaliana
ferredoxin-thioredoxin reductase
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Arabidopsis thaliana
FTR
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Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
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Arabidopsis thaliana

General Information

General Information Comment Organism
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