ATP Synthases in the Year 2000: Evolving Views about the Structures of These Remarkable Enzyme Complexes
- Cite this article as:
- Pedersen, P.L., Ko, Y.H. & Hong, S. J Bioenerg Biomembr (2000) 32: 325. doi:10.1023/A:1005594800983
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This introductory article briefly summarizes how our views about the structural features ofATP synthases (F0F1) have evolved over the past 30 years and also reviews some of our currentviews in the year 2000 about the structures of these remarkably unique enzyme complexes.Suffice it to say that as we approach the end of the first year of this new millinium, we canbe conservatively confident that we have a reasonably good grasp of the overall “low-resolution”structural features of ATP synthases. Electron microscopy techniques, combined with the toolsof biochemistry, molecular biology, and immunology, have played the leading role here byidentifying the headpiece, basepiece, central stalk, side stalk, cap, and in the mitochondrialenzyme, the collar around the central stalk. We can be reasonably confident also that we havea fairly good grasp of much of the “high-resolution” structural features of both the F1 moietycomprised of fives subunit types (α, β, γ, δ, and ∈) and parts of the F0 moiety comprised ofeither three (E. coli) or at least ten (mitochondria) subunit types. This information acquiredin several different laboratories, either by X-ray crystallography or NMR spectroscopy, includesdetails about the active site and subunit relationships. Moreover, it is consistent with recentlyreported data that the F1 moiety may be an ATP driven motor, which, during ATP synthesis,is driven in reverse by the electrochemical proton gradient generated by the electron transportchain. The real structural challenges of the future are to acquire at high resolution “complete”ATP synthase complexes representative of different stages of the catalytic cycle during ATPsynthesis and representative also of key regulatory states.