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| | ==Crystal structure of the human small CTD phosphatase 3 isoform 1== | | ==Crystal structure of the human small CTD phosphatase 3 isoform 1== |
| - | <StructureSection load='2hhl' size='340' side='right' caption='[[2hhl]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2hhl' size='340' side='right'caption='[[2hhl]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hhl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HHL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hhl]] is a 4 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=2HHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HHL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KEG:12-TUNGSTOPHOSPHATE'>KEG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ta0|1ta0]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KEG:12-TUNGSTOPHOSPHATE'>KEG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTDSPL, C3orf8, NIF1, NIFL, YA22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2hhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhl OCA], [https://pdbe.org/2hhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hhl RCSB], [https://www.ebi.ac.uk/pdbsum/2hhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hhl ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2hhl TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhl OCA], [http://pdbe.org/2hhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hhl RCSB], [http://www.ebi.ac.uk/pdbsum/2hhl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hhl ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2hhl TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CTDSL_HUMAN CTDSL_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 (By similarity). Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.<ref>PMID:15681389</ref> | + | [https://www.uniprot.org/uniprot/CTDSL_HUMAN CTDSL_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 (By similarity). Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.<ref>PMID:15681389</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Adams, J M]] | + | [[Category: Large Structures]] |
| - | [[Category: Almo, S C]] | + | [[Category: Adams JM]] |
| - | [[Category: Atwell, S]] | + | [[Category: Almo SC]] |
| - | [[Category: Bain, K T]] | + | [[Category: Atwell S]] |
| - | [[Category: Boice, A]] | + | [[Category: Bain KT]] |
| - | [[Category: Burley, S K]] | + | [[Category: Boice A]] |
| - | [[Category: Dickey, M]] | + | [[Category: Burley SK]] |
| - | [[Category: Emtage, S]] | + | [[Category: Dickey M]] |
| - | [[Category: Gheyi, T]] | + | [[Category: Emtage S]] |
| - | [[Category: Groshong, C]] | + | [[Category: Gheyi T]] |
| - | [[Category: Malashkevich, V N]] | + | [[Category: Groshong C]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Malashkevich VN]] |
| - | [[Category: Ozyurt, S]] | + | [[Category: Ozyurt S]] |
| - | [[Category: Powell, A]] | + | [[Category: Powell A]] |
| - | [[Category: Ramagopal, U]] | + | [[Category: Ramagopal U]] |
| - | [[Category: Reyes, C]] | + | [[Category: Reyes C]] |
| - | [[Category: Rooney, I]] | + | [[Category: Rooney I]] |
| - | [[Category: Rutter, M E]] | + | [[Category: Rutter ME]] |
| - | [[Category: Sauder, J M]] | + | [[Category: Sauder JM]] |
| - | [[Category: Schwinn, K D]] | + | [[Category: Schwinn KD]] |
| - | [[Category: Thompson, D A]] | + | [[Category: Thompson DA]] |
| - | [[Category: Toro, R]] | + | [[Category: Toro R]] |
| - | [[Category: Wasserman, S R]] | + | [[Category: Wasserman SR]] |
| - | [[Category: Ctd phosphatase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Keggins anion]]
| + | |
| - | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
Function
CTDSL_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 (By similarity). Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.
Structural genomics of protein phosphatases.,Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yeo M, Lee SK, Lee B, Ruiz EC, Pfaff SL, Gill GN. Small CTD phosphatases function in silencing neuronal gene expression. Science. 2005 Jan 28;307(5709):596-600. PMID:15681389 doi:10.1126/science.1100801
- ↑ Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK. Structural genomics of protein phosphatases. J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037 doi:http://dx.doi.org/10.1007/s10969-007-9036-1
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