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