PMID: 8334986

 

    Legend: Gene, Sites

Title : Three-dimensional structure of rat acid phosphatase

Abstract :

1. The crystal structure of recombinant rat prostatic acid phosphatase was determined to 3 A resolution with protein crystallographic methods
2. 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
3. Two disulfide bridges between residues 129-340 and 315-319 were found
4. Electron density at two of the glycosylation sites for parts of the carbohydrate moieties was observed
5. 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
6. Other subunit- subunit interactions involve conserved residues from loops between helices and beta-strands
7. The fold of the alpha/beta domain is similar to the fold observed in phosphoglycerate mutase
8. The active site is at the carboxy end of the parallel strands of the alpha/beta domain
9. There is a strong residual electron density at the phosphate binding site which probably represents a bound chloride ion
10. Biochemical properties and results from site-directed mutagenesis experiments of acid phosphatase are correlated to the three-dimensional structure

Output (sent_index, trigger, protein, sugar, site):

• 4. glycosylation, , -, -, sites

Output(Part-Of) (sent_index, protein, site):

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX