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    FEBS Lett. 2000 Apr 7;471(1):99-102.

    Soluble P-type ATPase from an archaeon, Methanococcus jannaschii.

    Ogawa H, Haga T, Toyoshima C.

    Source

    Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, Japan.

    Abstract

    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.

    PMID:
    10760521
    [PubMed - indexed for MEDLINE]

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