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    A new family of periplasmic-binding proteins that sense arsenic oxyanions

    Badilla Pino, Consuelo and Osborne, Thomas and Cole, Ambrose and Watson, C. and Djordjevic, S. and Santini, J.M. (2018) A new family of periplasmic-binding proteins that sense arsenic oxyanions. Scientific Reports 8 (1), p. 6282. ISSN 2045-2322.

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    Abstract

    Arsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that's role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate.

    Metadata

    Item Type: Article
    Additional Information: ** From Europe PMC via Jisc Publications Router. ** Licence for this article: cc by
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    SWORD Depositor: Mr Joe Tenant
    Depositing User: Mr Joe Tenant
    Date Deposited: 04 Jun 2018 13:39
    Last Modified: 29 Jul 2019 16:18
    URI: http://eprints.bbk.ac.uk/id/eprint/22528

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