EC Number   |
Reference |
|---|
   1.8.7.2 | mapping of the binding sites of ferredoxin for FTR by NMR using a gallium-substituted structural analog of ferredoxin. The interaction of erredoxin with FTR is in the slow to intermediate exchange regime. All of the residues with large chemical shift changes except I51 are located near the [2Fe-2S] loop |
703694 |
| 1.8.7.2 | Mössbauer spectroscopy study of both the as-purified and N-ethylmaleimide-modified forms of FTR demonstrate the presence of a unique iron site in the [4Fe-4S] cluster and suggest that site-specific cluster chemistry, involving the formation of a five-coordinate Fe site with two cysteinate ligands, occurs during catalytic cycling of FTR |
704156 |
| 1.8.7.2 | paramagnetic NMR spectroscopy study on the ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin. FTR uses distinct sites to bind ferredoxin and thioredoxin simultaneously to form a noncovalent ternary complex. Either a modest or major rotational movement of thioredoxin must take place when the noncovalent binary complex proceeds to the covalent complex |
704186 |
| 1.8.7.2 | purified transient complex between Fdx and GvDTR, 1.5fold molar excess of GvFdx1 over GvDTR, vapor diffusion method, mixing of protein in 10 mM Tris-HCl, pH 8.0, with an equal volume of mother liquor consisting of 40% v/v PEG 300, 100 mM sodium cacodylate-HCl, pH 6.5, and 200 mM sodium acetate, at 20°C, X-ray diffraction structure determination and analysis at 2.23-2.90 A resolution, molecular replacement using the crystal structures of GvDTR (PDB ID 5J60) and Fdx1 from Synechocystis (PDB ID 1OFF) as templates |
765599 |
| 1.8.7.2 | sitting drop vapor diffusion method, using 50 mM HEPES buffer (pH 7.5) and 1.7 M ammonium sulfate |
741911 |
| 1.8.7.2 | structures of FTR in both its one- and its two-electron-reduced intermediate states and of four complexes in the pathway. In the first complex of the pathway, ferredoxin-FTR, the ferredoxin [2Fe-2S] cluster is positioned suitably for electron transfer to the FTR [4Fe-4S] center. After the transfer of one electron, an intermediate is formed in which one sulfur atom of the FTR active site is free to attack a disulphide bridge in thioredoxin and the other sulfur atom forms a fifth ligand for an iron atom in the FTR [4Fe-4S] center. Ferredoxin then delivers a second electron that cleaves the FTR-thioredoxin heterodisulfide bond, which occurs in the ferredoxin-FTR-thioredoxin complex. In this structure, the redox centers of the three proteins are aligned to maximize the efficiency of electron transfer from the Fdx [2Fe-2S] cluster to the active-site disulfide of thioredoxin |
705878 |
| 1.8.7.2 | 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 |
765730 |
| 1.8.7.2 | to 2.8 A resolution, primitive cubic space group P23 or P213 |
723858 |
