1qfc

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[[Image:1qfc.jpg|left|200px]]<br /><applet load="1qfc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qfc.jpg|left|200px]]
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caption="1qfc, resolution 2.70&Aring;" />
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'''STRUCTURE OF RAT PURPLE ACID PHOSPHATASE'''<br />
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{{Structure
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|PDB= 1qfc |SIZE=350|CAPTION= <scene name='initialview01'>1qfc</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''STRUCTURE OF RAT PURPLE ACID PHOSPHATASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1QFC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFC OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10388567 10388567]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10388567 10388567]
[[Category: Acid phosphatase]]
[[Category: Acid phosphatase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: metal phosphatase]]
[[Category: metal phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:37 2008''

Revision as of 11:36, 20 March 2008


PDB ID 1qfc

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: , and
Activity: Acid phosphatase, with EC number 3.1.3.2
Coordinates: save as pdb, mmCIF, xml



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. 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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