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[[Image:1ute.jpg|left|200px]]
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{{STRUCTURE_1ute|  PDB=1ute  |  SCENE=  }}
'''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''


==PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE==
<StructureSection load='1ute' size='340' side='right'caption='[[1ute]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ute]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UTE 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]] 1.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=1ute FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ute OCA], [https://pdbe.org/1ute PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ute RCSB], [https://www.ebi.ac.uk/pdbsum/1ute PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ute ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPA5_PIG PPA5_PIG] Uteroferrin is a phosphoprotein phosphatase, synthesized in response to progesterone. It appears to function in transplacental transport of iron in pig.
== 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/ut/1ute_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ute ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. RESULTS: The 1.55 A resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched beta sheets flanked by alpha-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. CONCLUSIONS: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design.


==Overview==
Crystal structure of mammalian purple acid phosphatase.,Guddat LW, McAlpine AS, Hume D, Hamilton S, de Jersey J, Martin JL Structure. 1999 Jul 15;7(7):757-67. PMID:10425678<ref>PMID:10425678</ref>
BACKGROUND: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. RESULTS: The 1.55 A resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched beta sheets flanked by alpha-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. CONCLUSIONS: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1UTE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTE OCA].
</div>
<div class="pdbe-citations 1ute" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of mammalian purple acid phosphatase., Guddat LW, McAlpine AS, Hume D, Hamilton S, de Jersey J, Martin JL, Structure. 1999 Jul 15;7(7):757-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10425678 10425678]
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
[[Category: Acid phosphatase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Guddat, L W.]]
[[Category: De Jersey J]]
[[Category: Hamilton, S.]]
[[Category: Guddat LW]]
[[Category: Hume, D.]]
[[Category: Hamilton S]]
[[Category: Jersey, J De.]]
[[Category: Hume D]]
[[Category: Martin, J L.]]
[[Category: Martin JL]]
[[Category: Mcalpine, A.]]
[[Category: Mcalpine A]]
[[Category: Metalloenzyme]]
[[Category: Purple acid phosphatase]]
[[Category: Tartrate resistant acid phosphatase]]
[[Category: Uteroferrin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:39:48 2008''

Latest revision as of 00:34, 21 November 2024

PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE

1ute, resolution 1.55Å

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