|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of Rtt103 CTD-interacting domain bound to a Ser2Ser7 phosphorylated CTD peptide== | | ==Solution structure of Rtt103 CTD-interacting domain bound to a Ser2Ser7 phosphorylated CTD peptide== |
| - | <StructureSection load='5m9d' size='340' side='right'caption='[[5m9d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5m9d' size='340' side='right'caption='[[5m9d]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m9d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M9D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m9d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M9D FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTT103, YDR289C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5m9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9d OCA], [https://pdbe.org/5m9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m9d RCSB], [https://www.ebi.ac.uk/pdbsum/5m9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9d 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=5m9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9d OCA], [http://pdbe.org/5m9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m9d RCSB], [http://www.ebi.ac.uk/pdbsum/5m9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RT103_YEAST RT103_YEAST]] Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:15565157</ref> | + | [https://www.uniprot.org/uniprot/RT103_YEAST RT103_YEAST] Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:15565157</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jasnovidova, O]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kubicek, K]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Stefl, R]] | + | [[Category: Jasnovidova O]] |
| - | [[Category: Ctd-interacting domain]] | + | [[Category: Kubicek K]] |
| - | [[Category: Phosphorylation]] | + | [[Category: Stefl R]] |
| - | [[Category: Rnapii c-terminal domain]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
RT103_YEAST Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.[1] [2]
Publication Abstract from PubMed
RNA polymerase II contains a long C-terminal domain (CTD) that regulates interactions at the site of transcription. The CTD architecture remains poorly understood due to its low sequence complexity, dynamic phosphorylation patterns, and structural variability. We used integrative structural biology to visualize the architecture of the CTD in complex with Rtt103, a 3'-end RNA-processing and transcription termination factor. Rtt103 forms homodimers via its long coiled-coil domain and associates densely on the repetitive sequence of the phosphorylated CTD via its N-terminal CTD-interacting domain. The CTD-Rtt103 association opens the compact random coil structure of the CTD, leading to a beads-on-a-string topology in which the long rod-shaped Rtt103 dimers define the topological and mobility restraints of the entire assembly. These findings underpin the importance of the structural plasticity of the CTD, which is templated by a particular set of CTD-binding proteins.
Structure and dynamics of the RNAPII CTDsome with Rtt103.,Jasnovidova O, Klumpler T, Kubicek K, Kalynych S, Plevka P, Stefl R Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):11133-11138. doi:, 10.1073/pnas.1712450114. Epub 2017 Oct 4. PMID:29073019[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Scholes DT, Banerjee M, Bowen B, Curcio MJ. Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics. 2001 Dec;159(4):1449-65. PMID:11779788
- ↑ Kim M, Krogan NJ, Vasiljeva L, Rando OJ, Nedea E, Greenblatt JF, Buratowski S. The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II. Nature. 2004 Nov 25;432(7016):517-22. PMID:15565157 doi:http://dx.doi.org/nature03041
- ↑ Jasnovidova O, Klumpler T, Kubicek K, Kalynych S, Plevka P, Stefl R. Structure and dynamics of the RNAPII CTDsome with Rtt103. Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):11133-11138. doi:, 10.1073/pnas.1712450114. Epub 2017 Oct 4. PMID:29073019 doi:http://dx.doi.org/10.1073/pnas.1712450114
|
