Unique Structural and Functional Properties of A1A0 ATPase/Synthase from Archaea

Page: 309

M. Vidová and P. Šmigáň

Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Ivanka pri Dunaji, Slovak Republic


ATP synthases are present in every life form being the key enzymes of cellular bioenergetics. The enzyme from the Archaea forms a new class of ATPases, A1A0 ATP synthase. This enzyme has unusual structural and functional features, which separate it from F1F0 and V1V0 ATPases as a distinct enzyme class – A1A0 ATPase/synthase. It contains the transmembrane A0 domain and the cytoplasmatic A1 domain, including a specific site for ATP synthesis. The A1 domain is linked to the A0 part by D-subunit, a structural and functional analog of the γ-subunit of F1F0 ATPase. The genomic approach to the study of this enzyme combined with methods of molecular biology, biochemistry and structural biology, will extend the study of A1A0 ATPase/synthase and ATP synthesis to the molecular level.


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