Structural highlights
Function
[PPA5_RAT] May play a role in the process of bone resorption. The osteoclastic trap acts on nucleotide tri- and diphosphates with higher affinity, compared with other substrates.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tartrate-resistant acid phosphatase (TRAP) is a mammalian di-iron- containing enzyme that belongs to the family of purple acid phosphatases (PAP). It is highly expressed in a limited number of tissues, predominantly in bone-resorbing osteoclasts and in macrophages of spleen. We have determined the crystal structure of rat TRAP in complex with a phosphate ion to 2.7 A resolution. The fold resembles that of the catalytic domain of kidney bean purple acid phosphatase (KBPAP), although the sequence similarity is limited to the active site residues. A surface loop near the active site is absent due to proteolysis, leaving the active-site easily accessible from the surrounding solvent. This, we believe, gives a structural explanation for the observed proteolytic activation of TRAP. The current structure was determined at a relatively high pH and without any external reducing agents. It is likely that it represents an oxidized and therefore catalytically inactive form of the enzyme.
Crystal structure of a mammalian purple acid phosphatase.,Uppenberg J, Lindqvist F, Svensson C, Ek-Rylander B, Andersson G J Mol Biol. 1999 Jul 2;290(1):201-11. PMID:10388567[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Uppenberg J, Lindqvist F, Svensson C, Ek-Rylander B, Andersson G. Crystal structure of a mammalian purple acid phosphatase. J Mol Biol. 1999 Jul 2;290(1):201-11. PMID:10388567 doi:10.1006/jmbi.1999.2896
