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| | ==Crystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD phospho-Ser5 peptide== | | ==Crystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD phospho-Ser5 peptide== |
| - | <StructureSection load='4ygx' size='340' side='right' caption='[[4ygx]], [[Resolution|resolution]] 2.95Å' scene=''> | + | <StructureSection load='4ygx' size='340' side='right'caption='[[4ygx]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ygx]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ygx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YGX FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CG:(1R,2Z)-2-[(2R)-2-AMINO-3-(PHOSPHONOOXY)PROPYLIDENE]CYCLOPENTANECARBOXYLIC+ACID'>4CG</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CG:(1R,2Z)-2-[(2R)-2-AMINO-3-(PHOSPHONOOXY)PROPYLIDENE]CYCLOPENTANECARBOXYLIC+ACID'>4CG</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ygy|4ygy]], [[4yh1|4yh1]]</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=4ygx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ygx OCA], [https://pdbe.org/4ygx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ygx RCSB], [https://www.ebi.ac.uk/pdbsum/4ygx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ygx ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sym, CG2097 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Ssu72, CG14216, Dmel_CG14216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=4ygx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ygx OCA], [http://pdbe.org/4ygx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ygx RCSB], [http://www.ebi.ac.uk/pdbsum/4ygx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ygx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYMPK_DROME SYMPK_DROME]] Component of a protein complex required for cotranscriptional processing of 3'-ends of polyadenylated and histone pre-mRNA.<ref>PMID:18042462</ref> <ref>PMID:19450530</ref> | + | [https://www.uniprot.org/uniprot/SYMPK_DROME SYMPK_DROME] Component of a protein complex required for cotranscriptional processing of 3'-ends of polyadenylated and histone pre-mRNA.<ref>PMID:18042462</ref> <ref>PMID:19450530</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4ygx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4ygx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Symplekin|Symplekin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Mayfield, J E]] | + | [[Category: Large Structures]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Complex]] | + | [[Category: Mayfield JE]] |
| - | [[Category: Hydrolase]] | + | [[Category: Zhang Y]] |
| - | [[Category: Peptidomimetic]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| Structural highlights
Function
SYMPK_DROME Component of a protein complex required for cotranscriptional processing of 3'-ends of polyadenylated and histone pre-mRNA.[1] [2]
Publication Abstract from PubMed
Proline isomerization greatly impacts biological signaling but is subtle and difficult to detect in proteins. We characterize this poorly understood regulatory mechanism for RNA polymerase II carboxyl terminal domain (CTD) phosphorylation state using novel, direct, and quantitative chemical tools. We determine the proline isomeric preference of three CTD phosphatases: Ssu72 as cis-proline specific, Scp1 and Fcp1 as strongly trans-preferred. Due to this inherent characteristic, these phosphatases respond differently to enzymes that catalyze the isomerization of proline, like Ess1/Pin1. We demonstrate that this selective regulation of RNA polymerase II phosphorylation state exists within human cells, consistent with in vitro assays. These results support a model in which, instead of a global enhancement of downstream enzymatic activities, proline isomerases selectively boost the activity of a subset of CTD regulatory factors specific for cis-proline. This leads to diversified phosphorylation states of CTD in vitro and in cells. We provide the chemical tools to investigate proline isomerization and its ability to selectively enhance signaling in transcription and other biological contexts.
Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.,Mayfield JE, Fan S, Wei S, Zhang M, Li B, Ellington AD, Etzkorn FA, Zhang YJ ACS Chem Biol. 2015 Sep 15. PMID:26332362[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wagner EJ, Burch BD, Godfrey AC, Salzler HR, Duronio RJ, Marzluff WF. A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone pre-mRNA processing. Mol Cell. 2007 Nov 30;28(4):692-9. PMID:18042462 doi:10.1016/j.molcel.2007.10.009
- ↑ Sullivan KD, Steiniger M, Marzluff WF. A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Mol Cell. 2009 May 15;34(3):322-32. doi: 10.1016/j.molcel.2009.04.024. PMID:19450530 doi:10.1016/j.molcel.2009.04.024
- ↑ Mayfield JE, Fan S, Wei S, Zhang M, Li B, Ellington AD, Etzkorn FA, Zhang YJ. Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II. ACS Chem Biol. 2015 Sep 15. PMID:26332362 doi:http://dx.doi.org/10.1021/acschembio.5b00296
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