1QFC

STRUCTURE OF RAT PURPLE ACID PHOSPHATASE

Summary for 1QFC

• Entry DOI: 10.2210/pdb1qfc/pdb
• Descriptor: PROTEIN (PURPLE ACID PHOSPHATASE), 2-acetamido-2-deoxy-beta-D-glucopyranose, FE (III) ION, ... (4 entities in total)
• Functional Keywords: hydrolase, metal phosphatase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Lysosome: P29288
• Total number of polymer chains: 1
• Total formula weight: 34820.86

Authors

Uppenberg, J.,Lindqvist, F.,Svensson, C.,Ek-Rylander, B.,Andersson, G. (deposition date: 1999-04-08, release date: 2000-04-10, Last modification date: 2024-11-13)

Primary citation

Uppenberg, J.,Lindqvist, F.,Svensson, C.,Ek-Rylander, B.,Andersson, G.
Crystal structure of a mammalian purple acid phosphatase.
J.Mol.Biol., 290:201-211, 1999

PubMed Abstract: 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.

PubMed: 10388567
DOI: 10.1006/jmbi.1999.2896

Experimental method

X-RAY DIFFRACTION (2.7 Å)