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Literature summary extracted from

  • Takacs, E.; Barabas, O.; Petoukhov, M.V.; Svergun, D.I.; Vertessy, B.G.
    Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers (2009), FEBS Lett., 583, 865-871.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.23 expression of the core enzyme lacking the 28-residue-long C-terminal fly-specific segment Drosophila melanogaster
3.6.1.23 recombinant expression Homo sapiens
3.6.1.23 recombinant expression Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.23 purified recombinant core enzyme lacking the 28-residue-long C-terminal fly-specific segment, sitting drop vapor diffusion method, 0.002 ml of 3 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.0, also containing 50 mM NaCl and 1 mM DTT, 1.2 mM dUDP and 10 mM MgCl2 are mixed with an equal volume of reservoir solution containing 50 mM sodium succinate buffer, pH 4.6-4.8, and 200 mM NaCl and 30-35% v/v 2-methyl-2,4-pentanediol, 4°C, X-ray diffraction structure determination and analysis at 1.88 A resolution Drosophila melanogaster
3.6.1.23 purified recombinant enzyme Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.23 additional information mutations of a suggested hinge proline destabilize Escherichia coli dUTPase without preventing trimeric organization Escherichia coli
3.6.1.23 additional information mutations of a suggested hinge proline destabilize human dUTPase without preventing trimeric organization. But trimer formation is prevented in the human enzyme by truncating the C-terminus before the swapping arm Homo sapiens
3.6.1.23 additional information removal of the physiologically present, very flexible 28-residue C-terminal segment does not perturb catalytic function but facilitates crystallization Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.23 Drosophila melanogaster Q9V3I1
-
-
3.6.1.23 Escherichia coli P06968
-
-
3.6.1.23 Homo sapiens P33316
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.23 recombinant enzyme by ion exchange chromatography and gel filtration Homo sapiens

Subunits

EC Number Subunits Comment Organism
3.6.1.23 dimer hinge prolines play a role in oligomer assembly Drosophila melanogaster
3.6.1.23 homotrimer with interfaces formed between subunit surfaces, in the central channel, and by C-terminal beta-strand swapping. Analysis of intersubunit interactions reveals an important cohesive role for the C-terminus Homo sapiens
3.6.1.23 homotrimer with interfaces formed between subunit surfaces, in the central channel, and by C-terminal beta-strand swapping. Analysis of intersubunit interactions reveals an important cohesive role for the C-terminus Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.6.1.23 dUTP pyrophosphatase
-
 Homo sapiens
3.6.1.23 dUTP pyrophosphatase
-
 Drosophila melanogaster
3.6.1.23 dUTP pyrophosphatase
-
 Escherichia coli
3.6.1.23 dUTPase
-
 Homo sapiens
3.6.1.23 dUTPase
-
 Drosophila melanogaster
3.6.1.23 dUTPase
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.23 additional information
-
 heat-induced denaturation, unfolding is irreversible in all samples Homo sapiens