1ute
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1ute.png|left|200px]] | ||
- | < | + | ==PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE== |
- | + | <StructureSection load='1ute' size='340' side='right'caption='[[1ute]], [[Resolution|resolution]] 1.55Å' scene=''> | |
- | You may | + | == 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]] 1.55Å</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. | ||
- | + | 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> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1ute" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
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- | == | + | |
- | < | + | |
- | [[Category: | + | |
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
- | [[Category: | + | [[Category: De Jersey J]] |
- | [[Category: | + | [[Category: Guddat LW]] |
- | [[Category: | + | [[Category: Hamilton S]] |
- | [[Category: | + | [[Category: Hume D]] |
- | [[Category: Martin | + | [[Category: Martin JL]] |
- | [[Category: Mcalpine | + | [[Category: Mcalpine A]] |
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Current revision
PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE
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Categories: Large Structures | Sus scrofa | De Jersey J | Guddat LW | Hamilton S | Hume D | Martin JL | Mcalpine A