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New page: left|200px<br /><applet load="1qfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfc, resolution 2.70Å" /> '''STRUCTURE OF RAT PUR...
 
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[[Image:1qfc.jpg|left|200px]]<br /><applet load="1qfc" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1qfc.jpg|left|200px]]<br /><applet load="1qfc" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1qfc, resolution 2.70&Aring;" />
caption="1qfc, resolution 2.70&Aring;" />
'''STRUCTURE OF RAT PURPLE ACID PHOSPHATASE'''<br />
'''STRUCTURE OF RAT PURPLE ACID PHOSPHATASE'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1QFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG, FE and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFC OCA].  
1QFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFC OCA].  


==Reference==
==Reference==
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[[Category: metal phosphatase]]
[[Category: metal phosphatase]]


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