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

Teru Ogura, Sidney W. Whiteheart, Anthony J. Wilkinson

Research output: Contribution to journalArticlepeer-review

223 Scopus citations

Abstract

Arginines 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.

Original languageEnglish
Pages (from-to)106-112
Number of pages7
JournalJournal of Structural Biology
Volume146
Issue number1-2
DOIs
StatePublished - Apr 2004

Bibliographical note

Funding Information:
We thank one of the reviewers for particularly helpful input. This work was supported in part by grants from the Ministry of Education, Culture, Science, Sports and Technology, Japan to T.O., from the Japan Society for the Promotion of Science to T.O., from the National Institutes of Health (HL56652) to S.W.W., and from the BBSRC, UK (Grant 87/B13998) to A.J.W.

Keywords

  • AAA family
  • ATP hydrolysis
  • ATPase
  • Inter-subunit interactions

ASJC Scopus subject areas

  • Structural Biology

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