Abstract
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.
Original language | English (US) |
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Pages (from-to) | 93-114 |
Number of pages | 22 |
Journal | Annual Review of Biophysics and Biomolecular Structure |
Volume | 35 |
DOIs | |
State | Published - 2006 |
Keywords
- ATPase
- Molecular machines
- Motors
- Remodeling
ASJC Scopus subject areas
- Biophysics
- Structural Biology