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[[Image:1qfc.jpg|left|200px]]


{{Structure
==STRUCTURE OF RAT PURPLE ACID PHOSPHATASE==
|PDB= 1qfc |SIZE=350|CAPTION= <scene name='initialview01'>1qfc</scene>, resolution 2.70&Aring;
<StructureSection load='1qfc' size='340' side='right'caption='[[1qfc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
<table><tr><td colspan='2'>[[1qfc]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFC FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfc OCA], [https://pdbe.org/1qfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfc RCSB], [https://www.ebi.ac.uk/pdbsum/1qfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfc ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfc OCA], [http://www.ebi.ac.uk/pdbsum/1qfc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfc RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/PPA5_RAT 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/1qfc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qfc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


'''STRUCTURE OF RAT PURPLE ACID PHOSPHATASE'''
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<ref>PMID:10388567</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qfc" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Andersson G]]
[[Category: Andersson, G.]]
[[Category: Ek-Rylander B]]
[[Category: Ek-Rylander, B.]]
[[Category: Lindqvist F]]
[[Category: Lindqvist, F.]]
[[Category: Svensson C]]
[[Category: Svensson, C.]]
[[Category: Uppenberg J]]
[[Category: Uppenberg, J.]]
[[Category: hydrolase]]
[[Category: metal phosphatase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:40 2008''

Latest revision as of 23:47, 27 December 2023

STRUCTURE OF RAT PURPLE ACID PHOSPHATASE

1qfc, resolution 2.70Å

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