|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6npw' size='340' side='right'caption='[[6npw]], [[Resolution|resolution]] 2.49Å' scene=''> | | <StructureSection load='6npw' size='340' side='right'caption='[[6npw]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6npw]] 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=6NPW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NPW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6npw]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_RM11-1a Saccharomyces cerevisiae RM11-1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NPW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.486Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=6npw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6npw OCA], [https://pdbe.org/6npw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6npw RCSB], [https://www.ebi.ac.uk/pdbsum/6npw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6npw ProSAT]</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=6npw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6npw OCA], [http://pdbe.org/6npw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6npw RCSB], [http://www.ebi.ac.uk/pdbsum/6npw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6npw 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 == |
| Line 20: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6npw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6npw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Symplekin|Symplekin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Irani, S]] | + | [[Category: Saccharomyces cerevisiae RM11-1a]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Irani S]] |
| - | [[Category: Ctd of rna pol ii]] | + | [[Category: Zhang Y]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[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
The C-terminal domain of RNA polymerase II (CTD) contains a repetitive heptad sequence (YSPTSPS) whose phosphorylation states coordinate eukaryotic transcription by recruiting protein regulators. The precise placement and removal of phosphate groups on specific residues of the CTD are critical for the fidelity and effectiveness of RNA polymerase II-mediated transcription. During transcriptional elongation, phosphoryl-Ser5 (pSer5) is gradually dephosphorylated by CTD phosphatases, while Ser2 phosphorylation is accumulating. Using MS, X-ray crystallography, protein engineering, and immunoblotting analyses, here we investigated the structure and function of SSU72 homolog, RNA polymerase II CTD phosphatase (Ssu72, from Drosophila melanogaster), an essential CTD phosphatase that dephosphorylates pSer5 at the transition from elongation to termination, to determine the mechanism by which Ssu72 distinguishes the highly similar pSer2 and pSer5 CTDs. We found that Ssu72 dephosphorylates pSer5 effectively, but only has low activities toward pSer7 and pSer2. The structural analysis revealed that Ssu72 requires that the proline residue in the substrate's SP motif is in the cis configuration, forming a tight beta-turn for recognition by Ssu72. We also noted that residues flanking the SP motif, such as the bulky Tyr1 next to Ser2, prevent the formation of such configuration and enable Ssu72 to distinguish among the different SP motifs. The phosphorylation of Tyr-1 further prohibited Ssu72 binding to pSer2 and thereby prevented untimely Ser2 dephosphorylation. Our results reveal critical roles for Tyr1 in differentiating the phosphorylation states of Ser2/Ser5 of CTD in RNA polymerase II, which occur at different stages of transcription.
Structural determinants for accurate dephosphorylation of RNA polymerase II by its cognate CTD phosphatase during eukaryotic transcription.,Irani S, Sipe SN, Yang W, Burkholder NT, Lin B, Sim K, Matthews WL, Brodbelt JS, Zhang Y J Biol Chem. 2019 Apr 10. pii: RA119.007697. doi: 10.1074/jbc.RA119.007697. PMID:30971428[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
- ↑ Irani S, Sipe SN, Yang W, Burkholder NT, Lin B, Sim K, Matthews WL, Brodbelt JS, Zhang Y. Structural determinants for accurate dephosphorylation of RNA polymerase II by its cognate CTD phosphatase during eukaryotic transcription. J Biol Chem. 2019 Apr 10. pii: RA119.007697. doi: 10.1074/jbc.RA119.007697. PMID:30971428 doi:http://dx.doi.org/10.1074/jbc.RA119.007697
|
