Structure of the γ–ɛ complex of ATP synthase

ATP synthases (F1Fo-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency. Proton flow through Fo drives rotation of a ring of c-subunits and a complex of the γ and ɛ-subunits, causing cyclical conformational changes in F1 that are required for catalysis. The crystal structure of a large portion of F1 has been resolved. However, the structure of the central portion of the enzyme, through which conformational changes in Fo are communicated to F1, has until now remained elusive. Here we report the crystal structure of a complex of the ɛ-subunit and the central domain of the γ-subunit refined at 2.1 Å resolution. The structure reveals how rotation of these subunits causes large conformational changes in F1, and thereby provides new insights into energy coupling between Fo and F1.

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