Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
The crystal structure of recombinant rat prostatic acid phosphatase in complex with the inhibitor L(+)-tartrate was determined to 3-A resolution with protein crystallographic methods. The inhibitor binds at the carboxyl end of the parallel strands of the alpha/beta domain. One of the carboxyl groups of the tartrate molecule interacts with the conserved residues Arg-11, His-12, and Arg-15, which form part of the phosphate binding site. Furthermore, the C2 and C3 hydroxyl groups interact with His-257 and Arg-79. The second carboxyl group is close to Arg-79 but makes no direct hydrogen bonds to the protein. A sequence comparison between tartrate-sensitive and -resistant acid phosphatases suggests that these enzymes have different three-dimensional structures.
Lindqvist
Y
Y
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center.
Schneider
G
G
Vihko
P
P
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D013644:Tartrates / Q000737:chemistry*
D011994:Recombinant Proteins; D013644:Tartrates; D000135:Acid Phosphatase; C029768:tartaric acid