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

Abstract

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.