Purification and functional motifs of the recombinant ATPase of orf virus

• Published in: Protein expression and purification Vol. 79; no. 2; pp. 210 - 216
• Main Authors: Lin, Fong-Yuan, Chan, Kun-Wei, Wang, Chi-Young, Wong, Min-Liang, Hsu, Wei-Li
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.10.2011
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - isolation & purification; Adenosine Triphosphatases - metabolism; adenosine triphosphate; Adenosine Triphosphate - metabolism; adenosinetriphosphatase; Amino Acid Motifs - genetics; amino acid sequences; Animals; ATPase; calcium; Cloning, Molecular; Ecthyma, Contagious - virology; Escherichia coli; genes; guanosinetriphosphatase; Humans; Hydrolysis; ions; magnesium; Molecular Sequence Data; mutants; Orf virus; Orf virus - chemistry; Orf virus - enzymology; Orf virus - genetics; Parapoxvirus; Plasmids; Protein Structure, Tertiary; recombinant proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Sequence Deletion; Sheep - virology; Sheep Diseases - virology; Taiwan; Transformation, Bacterial; Viral Proteins - chemistry; Viral Proteins - genetics; Viral Proteins - isolation & purification; Viral Proteins - metabolism; Taiwan; ATPase; Orf virus; Parapoxvirus

Our previous study showed that the recombinant ATPase encoded by the A32L gene of orf virus displayed ATP hydrolysis activity as predicted from its amino acids sequence. This viral ATPase contains four known functional motifs (motifs I–IV) and a novel AYDG motif; they are essential for ATP hydrolysi...