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  • Crystal structures of sialyltransferase from Photobacterium damselae

    Author(s)
    Huynh, N
    Li, Y
    Yu, H
    Huang, S
    Lau, K
    Chen, X
    Fisher, AJ
    Griffith University Author(s)
    Lau, Kam
    Year published
    2014
    Metadata
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    Abstract
    Sialyltransferase structures fall into either GT-A or GT-B glycosyltransferase fold. Some sialyltransferases from the Photobacterium genus have been shown to contain an additional N-terminal immunoglobulin (Ig)-like domain. Photobacterium damselae a2-6-sialyltransferase has been used efficiently in enzymatic and chemoenzymatic synthesis of a2-6-linked sialosides. Here we report three crystal structures of this enzyme. Two structures with and without a donor substrate analog CMP-3F(a)Neu5Ac contain an immunoglobulin (Ig)-like domain and adopt the GT-B sialyltransferase fold. The binary structure reveals a non-productive ...
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    Sialyltransferase structures fall into either GT-A or GT-B glycosyltransferase fold. Some sialyltransferases from the Photobacterium genus have been shown to contain an additional N-terminal immunoglobulin (Ig)-like domain. Photobacterium damselae a2-6-sialyltransferase has been used efficiently in enzymatic and chemoenzymatic synthesis of a2-6-linked sialosides. Here we report three crystal structures of this enzyme. Two structures with and without a donor substrate analog CMP-3F(a)Neu5Ac contain an immunoglobulin (Ig)-like domain and adopt the GT-B sialyltransferase fold. The binary structure reveals a non-productive pre-Michaelis complex, which are caused by crystal lattice contacts that prevent the large conformational changes. The third structure lacks the Ig-domain. Comparison of the three structures
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    Journal Title
    FEBS Letters
    Volume
    588
    Issue
    24
    DOI
    https://doi.org/10.1016/j.febslet.2014.11.003
    Subject
    Medicinal and biomolecular chemistry
    Proteins and peptides
    Biochemistry and cell biology
    Evolutionary biology
    Publication URI
    http://hdl.handle.net/10072/67085
    Collection
    • Journal articles

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