title: Three-dimensional structure of rat acid phosphatase.
abstract: 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.
authors.affiliation: Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center.
authors.forename: G
authors.initials: G
authors.lastname: Schneider
authors.forename: Y
authors.initials: Y
authors.lastname: Lindqvist
authors.forename: P
authors.initials: P
authors.lastname: Vihko
mesh_terms: D000135:Acid Phosphatase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001665:Binding Sites; D001731:Bisphosphoglycerate Mutase / Q000737:chemistry; D002478:Cells, Cultured; D004583:Electrons; D006031:Glycosylation; D008297:Male; D008958:Models, Molecular; D009036:Moths; D011467:Prostate / Q000201:enzymology; D011487:Protein Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D000135:Acid Phosphatase; D001731:Bisphosphoglycerate Mutase