2km4: Difference between revisions
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<StructureSection load='2km4' size='340' side='right' caption='[[2km4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2km4' size='340' side='right' caption='[[2km4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2km4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2km4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KM4 FirstGlance]. <br> | ||
</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=4932 | </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=4932 ATCC 18824])</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=2km4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2km4 RCSB], [http://www.ebi.ac.uk/pdbsum/2km4 PDBsum]</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=2km4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km4 OCA], [http://pdbe.org/2km4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2km4 RCSB], [http://www.ebi.ac.uk/pdbsum/2km4 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2km4" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 18824]] | ||
[[Category: Becker, R]] | [[Category: Becker, R]] | ||
[[Category: Buratowski, S]] | [[Category: Buratowski, S]] | ||
Revision as of 11:13, 11 September 2015
Solution structure of Rtt103 CTD interacting domainSolution structure of Rtt103 CTD interacting domain
Structural highlights
Function[RT103_YEAST] Involved in transcription termination by RNA polymerase II and in regulation of Ty1 transposition.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPhosphorylation of the C-terminal domain (CTD) of RNA polymerase II controls the co-transcriptional assembly of RNA processing and transcription factors. Recruitment relies on conserved CTD-interacting domains (CIDs) that recognize different CTD phosphoisoforms during the transcription cycle, but the molecular basis for their specificity remains unclear. We show that the CIDs of two transcription termination factors, Rtt103 and Pcf11, achieve high affinity and specificity both by specifically recognizing the phosphorylated CTD and by cooperatively binding to neighboring CTD repeats. Single-residue mutations at the protein-protein interface abolish cooperativity and affect recruitment at the 3' end processing site in vivo. We suggest that this cooperativity provides a signal-response mechanism to ensure that its action is confined only to proper polyadenylation sites where Ser2 phosphorylation density is highest. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.,Lunde BM, Reichow SL, Kim M, Suh H, Leeper TC, Yang F, Mutschler H, Buratowski S, Meinhart A, Varani G Nat Struct Mol Biol. 2010 Oct;17(10):1195-201. Epub 2010 Sep 5. PMID:20818393[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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