1ute

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(New page: 200px<br /><applet load="1ute" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ute, resolution 1.55&Aring;" /> '''PIG PURPLE ACID PHOS...)
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[[Image:1ute.jpg|left|200px]]<br /><applet load="1ute" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ute, resolution 1.55&Aring;" />
 
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'''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''<br />
 
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==Overview==
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==PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE==
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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.
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<StructureSection load='1ute' size='340' side='right'caption='[[1ute]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ut/1ute_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1UTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with PO4, FEO and IPA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UTE OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10425678 10425678]
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</div>
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[[Category: Acid phosphatase]]
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<div class="pdbe-citations 1ute" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
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[[Category: Guddat, L.W.]]
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[[Category: Hamilton, S.]]
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[[Category: Hume, D.]]
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[[Category: Jersey, J.De.]]
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[[Category: Martin, J.L.]]
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[[Category: Mcalpine, A.]]
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[[Category: FEO]]
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[[Category: IPA]]
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[[Category: PO4]]
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[[Category: metalloenzyme]]
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[[Category: purple acid phosphatase]]
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[[Category: tartrate resistant acid phosphatase]]
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[[Category: uteroferrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:19:05 2007''
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==See Also==
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: De Jersey J]]
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[[Category: Guddat LW]]
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[[Category: Hamilton S]]
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[[Category: Hume D]]
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[[Category: Martin JL]]
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[[Category: Mcalpine A]]

Current revision

PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE

PDB ID 1ute

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