Evolutionary relationships and structural mechanisms of AAA+ proteins

Jan P. Erzberger, James M. Berger

Research output: Contribution to journalReview article

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 languageEnglish (US)
Pages (from-to)93-114
Number of pages22
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume35
DOIs
StatePublished - Jun 19 2006
Externally publishedYes

Keywords

  • ATPase
  • Molecular machines
  • Motors
  • Remodeling

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

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