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Biselyngbyasides (BLSs), macrolides from a marine cyanobacterium, are cytotoxic natural products whose target molecule is unknown. Here we report that BLSs are high affinity (K i ∼10nM) inhibitors of Ca 2+ -pumps with a unique binding mode. The crystal structures of the Ca 2+ -pump in complex with BLSs at 3.2–3.5Å-resolution show that BLSs bind to the pump near the cytoplasmic...
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...
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