AAA+ proteins: diversity in function, similarity in structure.

  title={AAA+ proteins: diversity in function, similarity in structure.},
  author={Jamie D. Snider and Walid A. Houry},
  journal={Biochemical Society transactions},
  volume={36 Pt 1},
The AAA+ (ATPases associated with various cellular activities) superfamily of proteins represents a distinct lineage of the larger class of P-loop NTPases. Members of this superfamily use the power of nucleotide binding and hydrolysis to direct molecular remodelling events. All AAA+ proteins share a common core architecture, which, through various sequence and structural modifications, has been adapted for use in a remarkably diverse range of functions. The following mini-review provides a… 

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The AAA+ superfamily of functionally diverse proteins
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AAA+ superfamily ATPases: common structure–diverse function
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  • Biology, Chemistry
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  • 2001
The AAA+ proteins represent a novel type of molecular chaperone and are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure.
Classification of AAA+ proteins.
Phylogenetic analysis of AAA proteins.
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The distribution of nucleotide specificity among the proteins of the G TPase superclass indicates that the common ancestor of the entire superclass was a GTPase and that a secondary switch to ATPase activity has occurred on several independent occasions during evolution.
Dissecting the Role of a Conserved Motif (the Second Region of Homology) in the AAA Family of ATPases
Analysis of the data in the light of the crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein suggests a plausible mechanism of ATP hydrolysis by the AAA ATPases, which invokes an intermolecular catalytic role for the SRH.
AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.
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