The Annual Review of Biophysics, in publication since 1972, covers significant developments in the field of Biophysics, including Macromolecular Structure, Function and Dynamics, Theoretical and Computational Biophysics, Molecular Biophysics of the Cell, Physical Systems Biology, Membrane Biophysics, Biotechnology, Nanotechnology, and Emerging Techniques.
Complex cellular events commonly depend on the activity of molecular “machines” that efficiently couple enzymatic and regulatory functions within a multiprotein assembly. An essential and expanding subset of these assemblies comprises proteins of the ATPases associated with diverse cellular activities (AAA+) family. The defining feature of AAA+ proteins is a structurally conserved ATP-binding module that oligomerizes into active arrays. ATP binding and hydrolysis events at the interface of neighboring subunits drive conformational changes within the AAA+ assembly that direct translocation or remodeling of target substrates. In this review, we describe the critical features of the AAA+ domain, summarize our current knowledge of how this versatile element is incorporated into larger assemblies, and discuss specific adaptations of the AAA+ fold that allow complex molecular manipulations to be carried out for a highly diverse set of macromolecular targets.