tji's Lutter:R [1 article]

Abstract

In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution, the three catalytic -subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the 33 subassembly relative to an -helical domain of the -subunit. ...