Structure and function of the AAA+ nucleotide binding pocket

Members of the diverse superfamily of AAA+ proteins are molecular machines responsible for a wide range of essential cellular processes. In this review we summarise structural and functional data surrounding the nucleotide binding pocket of these versatile complexes. Protein Data Bank (PDB) structur...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2012-01, Vol.1823 (1), p.2-14
Main Authors: Wendler, Petra, Ciniawsky, Susanne, Kock, Malte, Kube, Sebastian
Format: Article
Language:English
Subjects:
AAA+ ATPases
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - classification
Amino Acid Motifs
Animals
Binding Sites
Catalytic Domain
Conserved Sequence
Functional analysis
Humans
Hydrogen Bonding
Nucleotide binding pocket
Nucleotides - chemistry
Protein Binding
Protein Interaction Domains and Motifs
Structural analysis
Structural Homology, Protein
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Summary:Members of the diverse superfamily of AAA+ proteins are molecular machines responsible for a wide range of essential cellular processes. In this review we summarise structural and functional data surrounding the nucleotide binding pocket of these versatile complexes. Protein Data Bank (PDB) structures of closely related AAA+ ATPase are overlaid and biologically relevant motifs are displayed. Interactions between protomers are illustrated on the basis of oligomeric structures of each AAA+ subgroup. The possible role of conserved motifs in the nucleotide binding pocket is assessed with regard to ATP binding and hydrolysis, oligomerisation and inter-subunit communication. Our comparison indicates that in particular the roles of the arginine finger and sensor 2 residues differ subtly between AAA+ subgroups, potentially providing a means for functional diversification. This article is part of a Special Issue entitled: AAA ATPases: structure and function. ► We provide an overview of the current classification of AAA+ proteins. ► The characteristic features of the AAA+ nucleotide binding pocket are presented. ► We assemble biochemical data summarising the effects of site directed mutations in the nucleotide binding pocket. ► We assess the structural conservation of AAA+ domains and their nucleotide binding pockets. ► PDB structures of oligomeric AAA+ proteins are examined regarding protomer interactions at the nucleotide binding pocket.
ISSN:0167-4889
0006-3002
1879-2596
DOI:10.1016/j.bbamcr.2011.06.014