1qfc
From Proteopedia
(New page: 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=" | + | [[Image:1qfc.jpg|left|200px]]<br /><applet load="1qfc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qfc, resolution 2.70Å" /> | caption="1qfc, resolution 2.70Å" /> | ||
'''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- | + | 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:// | + | 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]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:51 2008'' |
Revision as of 12:38, 21 February 2008
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STRUCTURE OF RAT PURPLE ACID PHOSPHATASE
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.
About this Structure
1QFC is a Single protein structure of sequence from Rattus norvegicus with , and as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
Reference
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
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