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- W1996297669 abstract "An electron density map of crystalline alkaline phosphatase has been calculated to 7.7 Å resolution. The enzyme is present as a dimer on the 2-fold symmetry axis at 0, x, 16 in space group P3121. An orthorhombic form briefly examined is able to contain a tetrameric molecule with at least 2-fold symmetry. The location and environment of two zinc(II) ions has been determined in the dimer by an EDTA treatment of the crystalline enzyme. A small region of electron density located 10 Å from the zinc shifts by 8 Å when the metal is removed. The shift is reversed when zinc is added to the apoenzyme. Hg(II) binds preferentially at the vacant zinc site, and Hg(II) will also exchange with the zinc on the untreated enzyme. The slight 2 Å displacement of Hg from the zinc position may be related to the known inactivity of the mercury enzyme. The two Zn(II) ions are equivalent by symmetry. They are 32 Å apart and 16 Å from the dimer axis. This places them within the molecular envelope, but large channels leading inward from opposite sides of the dimer would allow a substrate molecule to come within 3 Å of a zinc ion. Also, there is space available for a substrate to lie on the dimer axis between the two ions, though 10 Å of protein density would be between the substrate and each zinc ion. In an inconclusive search for active site regions, the enzyme was exposed to p-iodophenylthiophosphate, 2-hydroxy-3-acetomercuri-5-nitrobenzyl-phosphonate, and arsenate ion." @default.
- W1996297669 created "2016-06-24" @default.
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- W1996297669 date "1973-03-01" @default.
- W1996297669 modified "2023-09-28" @default.
- W1996297669 title "A crystallographic study of alkaline phosphatase at 7.7 Å resolution" @default.
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- W1996297669 doi "https://doi.org/10.1016/0022-2836(73)90045-4" @default.
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