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1ta0

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(New page: 200px<br /> <applet load="1ta0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ta0, resolution 2.1&Aring;" /> '''Three-dimensional st...)
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[[Image:1ta0.gif|left|200px]]<br />
 
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<applet load="1ta0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ta0, resolution 2.1&Aring;" />
 
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'''Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand.'''<br />
 
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==Overview==
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==Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand.==
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Recycling of RNA polymerase II (Pol II) after transcription requires, dephosphorylation of the polymerase C-terminal domain (CTD) by the, phosphatase Fcp1. We report the X-ray structure of the small CTD, phosphatase Scp1, which is homologous to the Fcp1 catalytic domain. The, structure shows a core fold and an active center similar to those of, phosphotransferases and phosphohydrolases that solely share a DXDX(V/T), signature motif with Fcp1/Scp1. We demonstrate that the first aspartate in, the signature motif undergoes metal-assisted phosphorylation during, catalysis, resulting in a phosphoaspartate intermediate that was, structurally mimicked with the inhibitor beryllofluoride. Specificity may, result from CTD binding to a conserved hydrophobic pocket between the, active site and an insertion domain that is unique to Fcp1/Scp1. Fcp1, specificity may additionally arise from phosphatase recruitment near the, CTD via the Pol II subcomplex Rpb4/7, which is shown to be required for, binding of Fcp1 to the polymerase in vitro.
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<StructureSection load='1ta0' size='340' side='right'caption='[[1ta0]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ta0]] is a 1 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=1TA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TA0 FirstGlance]. <br>
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1TA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TA0 OCA].
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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]] 2.1&#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=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==Reference==
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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=1ta0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ta0 OCA], [https://pdbe.org/1ta0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ta0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ta0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ta0 ProSAT]</span></td></tr>
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Structure and mechanism of RNA polymerase II CTD phosphatases., Kamenski T, Heilmeier S, Meinhart A, Cramer P, Mol Cell. 2004 Aug 13;15(3):399-407. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15304220 15304220]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CTDS1_HUMAN CTDS1_HUMAN] Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.<ref>PMID:12721286</ref> <ref>PMID:15681389</ref>
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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/ta/1ta0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ta0 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cramer P]]
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[[Category: Cramer, P.]]
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[[Category: Heilmeier S]]
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[[Category: Heilmeier, S.]]
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[[Category: Kamenski T]]
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[[Category: Kamenski, T.]]
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[[Category: Meinhart T]]
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[[Category: Meinhart, T.]]
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[[Category: CIT]]
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[[Category: MG]]
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[[Category: alpha-beta protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:22:35 2007''
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Current revision

Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand.

PDB ID 1ta0

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