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5m48

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Coiled coil domain of Rtt103p

Structural highlights

5m48 is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.593Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5m48"

@@ Line 1: / Line 1: @@
 ==Coiled coil domain of Rtt103p==
-<StructureSection load='5m48' size='340' side='right' caption='[[5m48]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
+<StructureSection load='5m48' size='340' side='right'caption='[[5m48]], [[Resolution|resolution]] 2.59&Aring;' 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>
+<table><tr><td colspan='2'>[[5m48]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.593&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5m48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m48 OCA], [https://pdbe.org/5m48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m48 RCSB], [https://www.ebi.ac.uk/pdbsum/5m48 PDBsum], [https://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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
+[[Category: Large Structures]]
-[[Category: Jasnovidova, O]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Kalynych, S]]
+[[Category: Jasnovidova O]]
-[[Category: Plevka, P]]
+[[Category: Kalynych S]]
-[[Category: Stefl, R]]
+[[Category: Plevka P]]
-[[Category: Coiled coil]]
+[[Category: Stefl R]]
-[[Category: Dimer]]
-[[Category: Transcription]]

5m48

From Proteopedia

Current revision

Coiled coil domain of Rtt103p

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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