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  • Evidence of Ternary Complex Formation in Trypanosoma cruzi trans-Sialidase Catalysis

    Author(s)
    Oliveira, Isadora A
    Goncalves, Arlan S
    Neves, Jorge L
    von Itzstein, Mark
    Todeschini, Adriane R
    Griffith University Author(s)
    von Itzstein, Mark
    Year published
    2014
    Metadata
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    Abstract
    Trypanosoma cruzi trans-sialidase (TcTS) is a key target protein for Chagas disease chemotherapy. In this study, we investigated the implications of active site flexibility on the biochemical mechanism of TcTS. Molecular dynamics studies revealed remarkable plasticity in the TcTS catalytic site, demonstrating, for the first time, how donor substrate engagement with the enzyme induces an acceptor binding site in the catalytic pocket that was not previously captured in crystal structures. Furthermore, NMR data showed cooperative binding between donor and acceptor substrates, supporting theoretical results. In summary, our data ...
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    Trypanosoma cruzi trans-sialidase (TcTS) is a key target protein for Chagas disease chemotherapy. In this study, we investigated the implications of active site flexibility on the biochemical mechanism of TcTS. Molecular dynamics studies revealed remarkable plasticity in the TcTS catalytic site, demonstrating, for the first time, how donor substrate engagement with the enzyme induces an acceptor binding site in the catalytic pocket that was not previously captured in crystal structures. Furthermore, NMR data showed cooperative binding between donor and acceptor substrates, supporting theoretical results. In summary, our data put forward a coherent dynamic framework to understand how a glycosidase evolved its highly efficient trans-glycosidase activity.
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    Journal Title
    Journal of Biological Chemistry
    Volume
    289
    Issue
    1
    DOI
    https://doi.org/10.1074/jbc.M112.399303
    Subject
    Chemical sciences
    Proteins and peptides
    Biological sciences
    Biomedical and clinical sciences
    Publication URI
    http://hdl.handle.net/10072/67771
    Collection
    • Journal articles

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