Structural and mechanistic aspects of Amt/Rh proteins

Arnaud Javelle, Domenico Lupo, Xiao-Dan Li, Mike Merrick, Mohamed Chami, Pierre Ripoche, Fritz K Winkler

    Research output: Contribution to journalArticle

    50 Citations (Scopus)

    Abstract

    Amt/Rh proteins, which mediate movement of ammonium across cell membranes, are spread throughout the three kingdoms of life. Most functional studies on various members of the family have been performed using cellular assays in heterologous expression systems, which are, however, not very well suited for detailed mechanistic studies. Although now generally considered to be ammonia conducting channels, based on a number of experimental studies and structural insights, the possibility remains that some plant Amts facilitate net ammonium ion transport. The Escherichia coli channel AmtB has become the model system of choice for analysis of the mechanism of ammonia conductance, increasingly also through molecular dynamics simulations. Further progress in a more detailed mechanistic understanding of these proteins requires a reliable in vitro assay using purified protein, allowing quantitative kinetic measurements under a variety of experimental conditions for different Amt/Rh proteins, including mutants. Here, we critically review the existing functional data in the context of the most interesting and unresolved mechanistic questions and we present our results, obtained using an in vitro assay set up with the purified E. coli channel AmtB.
    Original languageEnglish
    Pages (from-to)472-81
    Number of pages10
    JournalJournal of Structural Biology
    Volume158
    Issue number3
    DOIs
    Publication statusPublished - 2007

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