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  • Crystal structure of mammalian purple acid phosphatase

    Author(s)
    Guddat, LW
    McAlpine, AS
    Hume, D
    Hamilton, S
    de Jersey, J
    Martin, JL
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    1999
    Metadata
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    Abstract
    Background: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. Results: The 1.55Å resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwichedβ sheets flanked byα-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. Conclusions: Despite less than 15% sequence identity, the ...
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    Background: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. Results: The 1.55Å resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwichedβ sheets flanked byα-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. Conclusions: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design.
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    Journal Title
    Structure
    Volume
    7
    Issue
    7
    DOI
    https://doi.org/10.1016/S0969-2126(99)80100-2
    Subject
    Biochemistry and Cell Biology not elsewhere classified
    Chemical Sciences
    Biological Sciences
    Information and Computing Sciences
    Publication URI
    http://hdl.handle.net/10072/347894
    Collection
    • Journal articles

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