Soluble P-type ATPase from an archaeon, Methanococcus jannaschii.
MJ0968 has been proposed to be an ancestor of P-type ATPase, because its primary structure is highly homologous to that of the core catalytic domain of P-type ATPase. However it completely lacks amino acid sequences that possibly constitute transmembrane domains. To examine if MJ0968 is indeed a P-type ATPase, it was overexpressed in Escherichia coli and purified. It did show ATPase activity, autophosphorylation and inhibition by vanadate. All these properties support the idea that MJ0968 is indeed a soluble P-type ATPase.
Ogawa
H
H
Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, Japan.
Haga
T
T
Toyoshima
C
C
D000251:Adenosine Triphosphatases / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D001345:Autoradiography; D001667:Binding, Competitive; D003001:Cloning, Molecular; D007700:Kinetics; D017017:Methanococcus / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D000251:Adenosine Triphosphatases; C109898:Zn(II)-translocating P-type ATPase