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mutant E138A bound to dTTP and mutant H121A bound to dCTP, hanging drop vapour diffusion method, 3.7 mg/ml E138A or 5.1 mg/ml H121A in 20 mM magnesium chloride, 50 mM HEPES, pH 6.8, and 5 mM nucleotide, mixing of 0.002 ml of protein solution with an equal volume of reservoir solution containing 34% PEG 400, 0.2 mM MgCl2, and 0.1 m HEPES, pH 7.5, equilibration against 1 ml of mother liquor, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.6-2.7 A resolution
recombinant mutant E138D in complex with dUTP, hanging drop vapour diffusion method, 0.002 ml of 2 mg/ml protein in solution with 5 mM dUTP and 20 mM MgSO4 is mixed with 0.002 ml reservoir solution containing 27.5% PEG 400, 50 mM MgSO4 and 0.1 M HEPES, pH 7.5, equilibration against 0.5 ml of reservoir solution, room temeprature, crystal X-ray diffraction structure determination and analysis at 2.1 A resolution
wild-type and mutant E138A, in complex with Mg2+ and dUTP, and dCTP
in complex with dTTP, hanging drop vapor diffusion method, using 200 mM lithium citrate and 20% (w/v) polyethylene glycol 4000
Halalkalibacterium halodurans
apoenzyme in complex with dCTP and with dUTP
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E138D
site-directed mutagenesis, the mutant enzyme shows a 140fold reduction in kcat and altered dTTP inhibition compared to the wild-type enzyme
E138Q
no enzymic activity, no change in overall structure compared to wild-type
H121A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
R115A
no enzymic activity, no change in overall structure compared to wild-type
R115Q
site-directed mutagenesis, inactive mutant
S111C
site-directed mutagenesis, inactive mutant
S111T
site-directed mutagenesis, the mutant enzyme shows a 30fold reduction in kcat and altered dTTP inhibition compared to the wild-type enzyme, modeling of the active site of the S111T enzyme, overview
V122G
site-directed mutagenesis, inactive mutant
E138A
no enzymic activity, no change in overall structure compared to wild-type
E138A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
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Mutational analysis of the nucleotide binding site of Escherichia coli dCTP deaminase
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Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme
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Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis
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Chloroviruses encode a bifunctional dCMP-dCTP deaminase that produces two key intermediates in dTTP formation
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Bacillus halodurans strain C125 encodes and synthesizes enzymes from both known pathways to form dump directly from cytosine deoxyribonucleotides
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