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

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JournalJOURNAL OF STRUCTURAL BIOLOGY
DatePublished - 2004
Issue number1-2
Volume146
Number of pages7
Pages (from-to)106-112
Original languageEnglish

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. (C) 2003 Elsevier Inc. All rights reserved.

    Research areas

  • AAA family, ATPase, ATP hydrolysis, inter-subunit interactions, JUNCTION BRANCH MIGRATION, ENHANCER-BINDING PROTEIN, ESCHERICHIA-COLI, IN-VITRO, MUTATIONAL ANALYSIS, CRYSTAL-STRUCTURE, COMPLEX, MECHANISM, MOTIF, FTSH

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