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5m48
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Coiled coil domain of Rtt103p== | |
| + | <StructureSection load='5m48' size='340' side='right' caption='[[5m48]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m48]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M48 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m48 OCA], [http://pdbe.org/5m48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m48 RCSB], [http://www.ebi.ac.uk/pdbsum/5m48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m48 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:29073019</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5m48" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
| + | [[Category: Jasnovidova, O]] | ||
| + | [[Category: Kalynych, S]] | ||
| + | [[Category: Plevka, P]] | ||
| + | [[Category: Stefl, R]] | ||
| + | [[Category: Coiled coil]] | ||
| + | [[Category: Dimer]] | ||
| + | [[Category: Transcription]] | ||
Revision as of 07:41, 8 November 2017
Coiled coil domain of Rtt103p
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