1s95: Difference between revisions

==Structure of serine/threonine protein phosphatase 5==

<StructureSection load='1s95' size='340' side='right'caption='[[1s95]], [[Resolution|resolution]] 1.60&Aring;' 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]] 1.6&#8491;</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>

[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.

[[Image:Consurf_key_small.gif|200px|right]]

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s9/1s95_consurf.spt"</scriptWhenChecked>

</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].

== 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>

==See Also==

*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]

== References ==

<references/>

</StructureSection>

[[Category: Large Structures]]

[[Category: Ciszak EM]]

[[Category: Honkanen RE]]

[[Category: Swingle MR]]