How proton pumps make ATP (original) (raw)

Nature Structural Biology volume 6, page 1090 (1999)Cite this article

If ATP is the universal currency of free energy in biological systems then the F1F0 ATP synthase is the mint. This enzyme can synthesize ATP using a transmembrane proton gradient. The ATP synthase is a multisubunit complex with a water-soluble F1 domain, the crystal structure of which has been solved, and a transmembrane F0 domain about which there is very little structural information. The F0 domain is made up of three types of subunits, in an _a_1_b_2 _c_12 stoichiometry. Low-resolution images and biochemical experiments suggest that the 12 c subunits are in a cylindrical arrangement with the a (purple) and b (not shown) subunits on the periphery. While it is clear that the F1 core subunit γ rotates during catalysis, the mechanism by which proton translocation through F0 is coupled to F1 subunit rotation is unknown.

Several models have been proposed in which ATP synthesis in the F1 domain is coupled to proton movement through F0 via movements of the c subunits. To explore this possibility, Rastogi and Girvin examined the structural changes induced by deprotonating a specific aspartic acid (Asp 61) on the c subunit known to be essential for proton transport (Nature; in the press). They combined their studies of the NMR structures of the deprotonated and protonated forms of the c subunit with distance constraints from crosslinking experiments to come up with a model for the _c_12 oligomer. The a subunit was modeled using biochemical data and then positioned with respect to the _c_12 oligomer using crosslinking data. Interestingly, this model places Asp 61 (shown in red and black) in a position to interact with Arg 210 (shown in blue and gray) in subunit a that is also essential for proton translocation.

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  1. Boyana Konforti

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Konforti, B. How proton pumps make ATP.Nat Struct Mol Biol 6, 1090 (1999). https://doi.org/10.1038/70013

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