4ygx: Difference between revisions
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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 [ | <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=' | </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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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: | [[Category: Drosophila melanogaster]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Mayfield JE]] | ||
[[Category: | [[Category: Zhang Y]] | ||
Revision as of 11:13, 3 May 2023
Crystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD phospho-Ser5 peptideCrystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD phospho-Ser5 peptide
Structural highlights
FunctionSYMPK_DROME Component of a protein complex required for cotranscriptional processing of 3'-ends of polyadenylated and histone pre-mRNA.[1] [2] Publication Abstract from PubMedProline 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 AlsoReferences
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