1.15.1.2: superoxide reductase
This is an abbreviated version!
For detailed information about superoxide reductase, go to the full flat file.
Word Map on EC 1.15.1.2
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1.15.1.2
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desulfovibrio
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non-heme
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gigas
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desulfoarculus
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baarsii
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sulfate-reducing
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high-spin
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radiolysis
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rubrerythrin
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hildenborough
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hydroperoxo
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peroxo
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square-pyramidal
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ferric-hydroperoxo
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thiolate-ligated
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rubredoxin-like
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feiii-ooh
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agriculture
- 1.15.1.2
- desulfovibrio
-
non-heme
- gigas
- desulfoarculus
- baarsii
-
sulfate-reducing
-
high-spin
-
radiolysis
- rubrerythrin
- hildenborough
-
hydroperoxo
-
peroxo
-
square-pyramidal
-
ferric-hydroperoxo
-
thiolate-ligated
-
rubredoxin-like
-
feiii-ooh
- agriculture
Reaction
Synonyms
1Fe SOR, 1Fe-SOR, 1Fe-superoxide reductase, 2Fe-SOR, class I SOR, class I superoxide reductase, class II SOR, cytochrome c–superoxide oxidoreductase, desulfoferrodoxin, desulforedoxin, Dfx, EC 1.18.96.1, Fe-SOR, GiSOR, MM_0632, More, neelaredoxin, neelaredoxin-type SOR, Nlr, PfSOR, rubredoxin oxidoreductase, SOR, superoxide reductase, TM0658, two-iron superoxide reductase, Zn/Fe-SOR
ECTree
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Crystallization
Crystallization on EC 1.15.1.2 - superoxide reductase
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purified recombinant enzyme, mixing of 0.0001 ml of 15 mg/ml protein in 20 mM phosphate buffer, pH 7.5, and 150 mM NaCl, with 0.0001 ml of reservoir solution, equilibration against 0.1 ml reservoir solution, vapour diffusion method, 2-3 days, method variantions, overview. X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution, MAD method
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crystal structure analysis of the wild-type and E114A mutant enzymes in different oxidation states, PDB IDs 2JI3, 2JI2, 2JI1, and 1VZI
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crystal structures determination of wild/tzp and mutant enzymes at 1.15-1.95 A resolution, PDB IDs 1VZI, 1VZG, 1VZH, 2JI1, 2JI2, and 2JI3
mutant E47A, alone and in complex with ferrocyanide, the iron in the actice site is coordinated through a bent cyano bridge
crystal structure analysis of the native and ferricyanide bound wild-type enzyme, PDB ID 1DFX
crystal structure determination at 1.9 A resolution, PDB ID 1DFX
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crystallization of the native enzyme, X-ray diffraction structure determination and analysis at 1.9 A resolution, modelling
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purified enzyme, hanging drop vapour diffusion technique, mixing of 0.001 ml of 12 mg/ml protein solution in a 1:1 ratio with reservoir solution, and equilibration against 0.1 ml reservoir solution, method optimization, best crystals are obtained after 1 d in 24% v/v dioxane at protein:precipitant ratios of 0.002:0.0001, 0.0025:0.0001 and 0.003:0.0001 ml, 35% w/v glycerol is added to the cover slip to avoid dioxane evaporation, to a final volume of 0.006-0.010 ml, X-ray diffraction structure determination and analysis at 1.9-2.65 A resolution, modeling
crystallization of purified recombinant oxidized 1Fe-SOR at room temperature, by sitting-drop vapour-diffusion method, mixing of 15 mg/ml protein in 20 mM Tris-HCl pH 7.2, 150 mM NaCl, with different drop mixing ratios of protein and reservoir solutions, method optimization to hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution with 0.0005 ml of reservoir solution containing 85 mM Tris, pH 8.5, 8.5 mM NiCl2, 15% v/v PEG 2000 MME, and 15% v/v glycerol, X-ray diffraction structure determination and analysis of the blue crystals at 2.4 A resolution
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crystal structure analysis of the reduced or the oxidized and Glu bound wild-type enzyme, PDB IDs 1DQI, 1DO6, and 1DQK
crystal structure determination at 2.0 A and 1.7 A resolution, respectively, PDB IDs 1DO6 and 1DQI
crystal structure analysis of the oxidized and Glu bound wild-type enzyme, PDB ID 2HVB
crystal structure determination at 2.5 A resolution, PDB ID 2HVB
crystal structure analysis of the reduced wild-type enzyme, PDB ID 2AMU
crystal structure determination at 2.0 A and 1.1 A resolution, respectively, PDB IDs 2AMU and 3QZB
crystal structure analysis of the native and Glu unbound wild-type enzyme, PDB ID 1Y07
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in presence of polyethylene glycol and magnesium chloride. Crystals grown in presence of K3Fe(CN)6 belong to space group P21 and diffract belong 1.6 A resolution, crystals grown in presence of Na2IrCl6 belong to space group C2 and diffract beyond 1.55 A
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protein lacks the N-terminal domain with the desulforedoxin-type iron centre known from other soperoxide reductases. Lack of the iron centre causes a decrease in the cohersion of the domain and some disorder. The C-terminal domain shows the characteristic immunoglobulin-like fold and harbours the Fe(His)4(cys) active centre
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