title: Structure and function of the AAA+ nucleotide binding pocket.
abstract: 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.
authors.affiliation: Gene Center, Ludwig-Maximilians-Universität München, München, Germany. wendler@genzentrum.lmu.de
authors.forename: Petra
authors.initials: P
authors.lastname: Wendler
authors.forename: Susanne
authors.initials: S
authors.lastname: Ciniawsky
authors.forename: Malte
authors.initials: M
authors.lastname: Kock
authors.forename: Sebastian
authors.initials: S
authors.lastname: Kube
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000145:classification; D020816:Amino Acid Motifs; D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain; D017124:Conserved Sequence; D006801:Humans; D006860:Hydrogen Bonding; D009711:Nucleotides / Q000737:chemistry; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D040681:Structural Homology, Protein
chemical_list: D009711:Nucleotides; D000251:Adenosine Triphosphatases