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  • Endosialidase NF Appears To Bind PolySia DP5 in a Helical Conformation

    Author(s)
    Haselhorst, Thomas
    Stummeyer, Katharina
    Muehlenhoff, Martina
    Schaper, Wiebke
    Gerardy-Schahn, Rita
    von Itzstein, Mark
    Griffith University Author(s)
    von Itzstein, Mark
    Haselhorst, Thomas E.
    Schaper, Wiebke
    Year published
    2006
    Metadata
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    Abstract
    Phages infecting the polySia-encapsulated human pathogen E. coli K1 are equipped with capsule-degrading tail spikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. The X-ray crystallographic structure of endosialidase has been reported but it remains unclear how polySia interacts with the active site. Here we report STD and trNOE NMR experiments that investigate the binding mode of polySia DP5 at a molecular level.Phages infecting the polySia-encapsulated human pathogen E. coli K1 are equipped with capsule-degrading tail spikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. The X-ray crystallographic structure of endosialidase has been reported but it remains unclear how polySia interacts with the active site. Here we report STD and trNOE NMR experiments that investigate the binding mode of polySia DP5 at a molecular level.
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    Journal Title
    ChemBioChem
    Volume
    7
    Publisher URI
    http://www3.interscience.wiley.com/journal/72510898/home
    DOI
    https://doi.org/10.1002/cbic.200600252
    Copyright Statement
    © 2006 John Wiley & Sons, Ltd. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the author for more information.
    Subject
    Medicinal and Biomolecular Chemistry
    Biochemistry and Cell Biology
    Publication URI
    http://hdl.handle.net/10072/13721
    Collection
    • Journal articles

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