Abstract
A key component in cellular bioenergetics is the ATP synthase. The enzyme from archaea represents a new class of ATPases, the A 1A O ATP synthases. They are composed of two domains that function as a pair of rotary motors connected by a central and peripheral stalk(s). The structure of the chemically-driven motor (A 1) was solved by small angle X-ray scattering in solution, and the structure of the first A 1A O ATP synthases (from methanoarchaea) was obtained recently by single particle analyses. These studies revealed novel structural features such as a second peripheral stalk and a collar-like structure. Interestingly, the membrane-embedded electrically-driven motor (A O) is very different in archaea with sometimes novel, exceptional subunit composition.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Bioenergetics
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