Crystal structure of mammalian purple acid phosphatase

Luke W Guddat, Alan S McAlpine, David Hume, Susan Hamilton, John de Jersey, Jennifer L Martin
<span title="">1999</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="" style="color: black;">Structure</a> </i> &nbsp;
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 1.55 Å resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched β sheets flanked by α-helical segments. The molecule shows internal symmetry, with
more &raquo; ... 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. Addresses:
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="">doi:10.1016/s0969-2126(99)80100-2</a> <a target="_blank" rel="external noopener" href="">pmid:10425678</a> <a target="_blank" rel="external noopener" href="">fatcat:sjhkulzrhnd2dpbcl3adrzdvoe</a> </span>
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