Literature summary for 3.6.1.23 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.

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
purified recombinant enzyme	Homo sapiens

Crystallization (Comment)

Organism

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

purified recombinant enzyme

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	mutations of a suggested hinge proline destabilize Escherichia coli dUTPase without preventing trimeric organization	Escherichia coli
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
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

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

Purification (Commentary)

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

Subunits

Subunits	Comment	Organism
dimer	hinge prolines play a role in oligomer assembly	Drosophila melanogaster
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
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

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

Temperature Stability [°C]

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