1qfc: Difference between revisions
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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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== | ==STRUCTURE OF RAT PURPLE ACID PHOSPHATASE== | ||
Tartrate-resistant acid phosphatase (TRAP) is a mammalian di-iron- | <StructureSection load='1qfc' size='340' side='right'caption='[[1qfc]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== 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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1qfc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Andersson G]] | |||
[[Category: Andersson | [[Category: Ek-Rylander B]] | ||
[[Category: Ek-Rylander | [[Category: Lindqvist F]] | ||
[[Category: Lindqvist | [[Category: Svensson C]] | ||
[[Category: Svensson | [[Category: Uppenberg J]] | ||
[[Category: Uppenberg | |||
Latest revision as of 23:47, 27 December 2023
STRUCTURE OF RAT PURPLE ACID PHOSPHATASE
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