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Three‐dimensional structure of rat acid phosphatase.
Author(s) -
Schneider G.,
Lindqvist Y.,
Vihko P.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb05921.x
Subject(s) - biological sciences , library science , center (category theory) , biology , chemistry , computational biology , crystallography , computer science
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.