Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases.

TitleConserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases.
Publication TypeJournal Article
Year of Publication2004
JournalJournal of structural biology
Volume146
Issue1-2
Pagination106-12
Date Published2004 Apr-May
ISSN1047-8477
AbstractArginines are a recurrent feature of the active sites and subunit interfaces of the ATPase domains of AAA and AAA+ proteins. In particular family members these residues occupy two or more, of four key sites in the vicinity of the ATP cofactor, where they transduce the chemical events of ATP binding and hydrolysis into a mechanochemical outcome. Structural and biochemical analyses have led to the proposal of molecular mechanisms in which these conserved arginines play crucial roles. Comparative studies, however, point to functional divergence for each of these conserved arginines. In this review, we will discuss what is known about these critical arginines and what can be concluded about their role in the function of AAA and AAA+ proteins.
PubMed Linkhttp://www.ncbi.nlm.nih.gov/pubmed/15095758?dopt=Abstract
Short TitleJ Struct Biol