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1.18.1.2: ferredoxin-NADP+ reductase

This is an abbreviated version!
For detailed information about ferredoxin-NADP+ reductase, go to the full flat file.

Word Map on EC 1.18.1.2

Reaction

2 reduced ferredoxin +

NADP+
+
H+
= 2 oxidized ferredoxin +
NADPH

Synonyms

ABO_0145, adrenodoxin reductase, AnFNR, BsFNR, CT1512, cytochrome b6f -associated ferredoxin:NADP+ oxidoreductase, DA1, EC 1.6.7.1, EC 1.6.99.4, Fd-NADP+ reductase, ferredoxin (flavodoxin)-(reduced) nicotinamide adenine dinucleotide phosphate reductase, ferredoxin (flavodoxin)-NAD(P)H reductase, ferredoxin (flavodoxin)-NADP(H) reductase, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin NADP oxidoreductase, ferredoxin NADP reductase, ferredoxin NADP(H) oxidoreductase, ferredoxin NADP+ oxidoreductase, ferredoxin NADP+ reductase, ferredoxin nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-NAD(P)+ oxidoreductase, ferredoxin-NAD(P)+ reductase, ferredoxin-NAD(P)H reductase, ferredoxin-NADP oxidoreductase, ferredoxin-NADP reductase, Ferredoxin-NADP(+) reductase, ferredoxin-NADP(H) oxidoreductase, ferredoxin-NADP(H) reductase, ferredoxin-NADP+ oxidoreductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+-oxidoreductase, ferredoxin-NADP+-reductase, ferredoxin-NADP-oxidoreductase, ferredoxin-NADP-reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase, ferredoxin-TPN reductase, ferredoxin: NADP(+) oxidoreductase, ferredoxin: NADP+ oxidoreductase, ferredoxin:NADP oxidoreductase, ferredoxin:NADP(+) oxidoreductase, ferredoxin:NADP(H) oxidoreductase, ferredoxin:NADP(H) oxidoreductase 2, ferredoxin:NADP+ oxidoreductase, ferredoxin:NADP+ reductase, ferredoxin:NADPH oxidoreductase, ferric reductase, Flavodoxin reductase, FLDR, FLXR, FNR, FNR-A, FNR-B, FNR1, FNR2, FNRII, FNRL, FNRS, FPR, FprA, FprB, Fprs, LFNR1, LFNR2, mitochondrial-type ferredoxin:NADP+ reductase, More, mtFNR, NADH-dependent reduced ferredoxin:NADP oxidoreductase, NADP:ferredoxin oxidoreductase, NADPH ferredoxin reductase, NADPH-dependent ferredoxin reductase, NADPH:ferredoxin oxidoreductase, NfnAB, NfnIII, NFR, PETH, PfFNR, pFNR, photosynthetic ferredoxin NADP+ oxidoreductase, photosynthetic FNR, plastidic-type ferredoxin-NADP+ reductase, PP4_41290, RcFPR, reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate, RFNR2, ST2133, TgFNR, TPNH-ferredoxin reductase, YumC

ECTree

     1 Oxidoreductases
         1.18 Acting on iron-sulfur proteins as donors
             1.18.1 With NAD+ or NADP+ as acceptor
                1.18.1.2 ferredoxin-NADP+ reductase

Crystallization

Crystallization on EC 1.18.1.2 - ferredoxin-NADP+ reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with NADP+, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
Interactions between FNR and the putative protein partners, ferredoxin Fd and flavodoxin Fld, were modeled, using surface energy analysis, computational rigid-body docking simulations, and interface side-chain refinement. The results suggest the existence of alternative binding modes in these electron transfer proteins.
model of enzyme:flavodoxin complex based on crystal structures. Key participation of residues K75 and K72 in complex formation with both ferredoxin and flavodoxin
-
mutant
-
purified recombinant mutant E139K, hanging drop vapour diffusion method, 0.002 ml protein solution containing 0.75 mM protein in 10 mM Tris-HCl, pH 8.0, plus 0.001 ml reservoir solution containing 5% w/v beta-octylglycoside, 18% PEG 6000, 20 mM ammonium sulfate, and 0.1 M MES/NaOH, pH 5.5, equilibration against 1 ml reservoir solution at 20°C, phase separation due to detergent, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
purified recombinant mutant enzymes L263P, T155G/A160T, and T155G/A160T/L263P, hanging drop method, 0.002 ml of protein solution, containing 0.75 mM protein, 10 mM Tris-HCl, pH 8.0, plus 0.001 ml of unbuffered 5% w/v beta-octyl-glycoside solution, plus 0.002 ml reservoir solution, containing 18-20% w/v PEG 6000, 20 mM ammonium sulfate, 0.1 M MES-NaOH, pH 5.0, equilibration against 1 ml reservoir solution at 20°C, 1-7 days, phase separation caused by detergent, X-ray diffraction structure determination and analysis at 1.63-2.15
FNR in complex with NADP+, two different crystal forms, mixing of 0.001 ml of 10 mg/ml protein and 2.5 mM NADP+ with 0.001 ml of reservoir solution containing 0.1 M HEPES buffer, pH 7.5, 30% 1,2-propanediol, and 20% PEG 400 for form I, and 20% PEG 3350, 0.2 M sodium fluoride, and 5% trehalose for form II, 20°C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, respetively, molecular replacement
purified recombinant FNR in complex with NADP+ in two different forms, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl pH 8.0, 200 mM NaCl, and 2.5 mM NADP+, is mixed with 0.001 ml reservoir solution, 20°C. The reservoir solutions consist of 0.1 M HEPES buffer pH 7.5, 30% 1,2-propanediol, 20% PEG 400 for form I, and of 20% PEG 3350, 0.2 M sodium fluoride and 5% trehalose for form II. X-ray diffraction structure determination and analysis at 1.8 and 1.9 A resolution, respectively, molecular replacement, modelling
-
crystal structure determination and analysis at 2.5 A resolution
-
hanging drop vapour diffusion method, using 0.1 M MES buffer pH 5.8 containing 16% (w/v) PEG 6K and 0.1 M ammonium sulfate as precipitant
-
mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed
diffraction to 2.4 A, space group P21
-
using 27% PEG 3350, 50 mM Tris-HCl buffer pH 7.0, at 18°C
a multiscale modelling approach for analysis of the electron transfer process in complexes of the enzyme with both ferredoxin and flavodoxin, reactions of EC 1.19.1.1 and EC1.18.1.2, respectively. The electron transfer in FNR/ferredoxin proceedes through a bridge-mediated mechanism in a dominant protein-protein complex, where transfer of the electron is facilitated by ferredoxin loop-residues 40-49. In FNR/flavodoxin, a direct transfer between redox cofactors is observed and less complex specificity than in ferredoxin
analysis of the enzyme in complex with a synthetic peptide representing the first FNR-binding repeat from Pisum sativum Tic62, including the strictly conserved core motif KTEQPLSPYTAYDDLKPPSSPSPTKPS, based on the crystal structure PDB ID 1QG0, X-ray diffraction structure analysis at 1.7 A resolution, molecular replacement
-
crystallizations of wild-type enzyme, ferredoxin-complexed enzyme, and enzyme mutants Y308S, complexed with NADP+ or NADPH, and Y308W, complexed with NADP+, crystal structure determinations and analysis at 1.7-2.5 A resolution, overview
-
mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed
free enzyme and in complex with 2’-phospho-AMP. Structures reveal a covalent dimer, which relies on the oxidation of residue C99 in two opposing subunits, and a helix-coil transition that occurs in the NADP-binding domain, triggered by 2’-phospho-AMP binding. Studies in solution show that NADP+, as well as 2’-phospho-AMP, promotes the formation of the disulfide-stabilized dimer. The dimer is inactive, but full activity is recovered upon disulfide reduction
in free form and in complex with 2'-phospho-AMP, in 22-25% PEG 4000, 0.1 M sodium cacodylate (pH 6.0), 0.2 M sodium acetate
space group P21
-
hanging drop vapour diffusion method, in 200 mM ammonium acetate, 100 mM sodium citrate tribasic dihydrate, and 25% (v/v) PEG-4000 (pH 5.6)
-
homology modeling of wild-type and mutants K259A, K259D. In the wild-type, the Lys259 residue is located close to the FAD cofactor. Lys258 makes van der Waals contacts to the ribose of FAD
vapor diffusion method, using 0.22 M magnesium sulfate, 27% (w/v) polyethylene glycol 3350, and 0.4% (v/v) ethyl acetate in the presence of 1 mM sodium dithionite
in complex with 2'-phospho-AMP and NADP+. In the complexes obtained, the nucleotides bind exclusively through the adenosine moiety. The adenosine moiety binds into a cavity formed by residues of conserved segments, i.e residues 128 to 130, residues 158 to 163, residues 193 to 205, and residues 233 to 240. The adenosine binding site is essentially formed by residues R158, R195 and R203, which stabilise the nucleotide
recombinant enzyme, hanging drop vapour diffusion method in presence of n-heptyl-beta-D-thioglucoside which is required for stabilization of the disordered regions of the protein, 18°C, X-ray diffraction structure determination and analysis, at 1.8 A resolution
-
crystallizations of oxidized enzyme, dithionite-reduced enzyme, 2',5'-ADP-complexed enzyme, enzyme mutants S96V, E312A, E312L, and E312Q, crystal structure determinations and analysis at 1.7-2.0 A resolution, overview
-
purified recombinant NfnAB free or in complex with NADH, sitting drop vapour diffusion method, 17.5 mg/ml NfnAB protein in 10 mM MOPS-KOH, pH 7.0, 2 mM DTT, and 0.01 mM FAD, room temperature, for the complex soaking the crystals with 5mM NADH for 40 min, multiple wavelength anomalous dispersion X-ray diffraction structure determinatin and analysis at 2.3-2.4 A resolution, modeling
-
homology modeling of wild-type and mutant S267R in complex with ferredoxin. Mutant shows major sterical and electrostatical effects on the FAD function as well as on residues Y266, I268 and Y497 neighbouring the mutation
-
crystallizations of wild-type enzyme, oxidized, or substrate-complexed, and of diverse enzyme mutants, crystal structure determination and analysis at 1.6-2.5 A resolution, overview
-
crystal structure determination and analysis of leaf enzyme, free or complexed with ferredoxin, and root enzyme at 2.2-2.6 and 1.7 A resolution, respectively
-
hanging drop vapor diffusion method, using 20% (w/v) PEG6000, 100 mM sodium cacodylate, pH 6.5