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Title
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Three-dimensional structure of rat acid phosphatase.
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Authors
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G.Schneider,
Y.Lindqvist,
P.Vihko.
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Ref.
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Embo J, 1993,
12,
2609-2615.
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PubMed id
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Abstract
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The crystal structure of recombinant rat prostatic acid phosphatase was
determined to 3 A resolution with protein crystallographic methods. The enzyme
subunit is built up of two domains, an alpha/beta domain consisting of a
seven-stranded mixed beta-sheet with helices on both sides of the sheet and a
smaller alpha domain. Two disulfide bridges between residues 129-340 and 315-319
were found. Electron density at two of the glycosylation sites for parts of the
carbohydrate moieties was observed. The dimer of acid phosphatase is formed
through two-fold interactions of edge strand 3 from one subunit with strand 3
from the second subunit, thus extending the beta-sheet from seven to 14 strands.
Other subunit-subunit interactions involve conserved residues from loops between
helices and beta-strands. The fold of the alpha/beta domain is similar to the
fold observed in phosphoglycerate mutase. The active site is at the carboxy end
of the parallel strands of the alpha/beta domain. There is a strong residual
electron density at the phosphate binding site which probably represents a bound
chloride ion. Biochemical properties and results from site-directed mutagenesis
experiments of acid phosphatase are correlated to the three-dimensional
structure.
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