1s95
From Proteopedia
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(New page: 200px<br /> <applet load="1s95" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s95, resolution 1.60Å" /> '''Structure of serine...) |
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| - | [[Image:1s95.gif|left|200px]]<br /> | ||
| - | <applet load="1s95" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1s95, resolution 1.60Å" /> | ||
| - | '''Structure of serine/threonine protein phosphatase 5'''<br /> | ||
| - | == | + | ==Structure of serine/threonine protein phosphatase 5== |
| - | Serine/threonine protein phosphatase-5 (PP5) affects many signaling | + | <StructureSection load='1s95' size='340' side='right'caption='[[1s95]], [[Resolution|resolution]] 1.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1s95]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S95 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]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=1s95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s95 OCA], [https://pdbe.org/1s95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s95 RCSB], [https://www.ebi.ac.uk/pdbsum/1s95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s95 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PPP5_HUMAN PPP5_HUMAN] May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1. | ||
| + | == 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/s9/1s95_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=1s95 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Serine/threonine protein phosphatase-5 (PP5) affects many signaling networks that regulate cell growth and cellular responses to stress. Here we report the crystal structure of the PP5 catalytic domain (PP5c) at a resolution of 1.6 A. From this structure we propose a mechanism for PP5-mediated hydrolysis of phosphoprotein substrates, which requires the precise positioning of two metal ions within a conserved Asp271-M1:M2-W1-His427-His304-Asp274 catalytic motif (where M1 and M2 are metals and W1 is a water molecule). The structure of PP5c provides a structural basis for explaining the exceptional catalytic proficiency of protein phosphatases, which are among the most powerful known catalysts. Resolution of the entire C terminus revealed a novel subdomain, and the structure of the PP5c should also aid development of type-specific inhibitors. | ||
| - | + | Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5.,Swingle MR, Honkanen RE, Ciszak EM J Biol Chem. 2004 Aug 6;279(32):33992-9. Epub 2004 May 23. PMID:15155720<ref>PMID:15155720</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1s95" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ciszak EM]] | ||
| + | [[Category: Honkanen RE]] | ||
| + | [[Category: Swingle MR]] | ||
Current revision
Structure of serine/threonine protein phosphatase 5
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