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5lvf

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Revision as of 18:51, 18 October 2023

Solution structure of Rtt103 CTD-interacting domain bound to a Thr4 phosphorylated CTD peptide

Structural highlights

5lvf is a 2 chain structure with sequence from Saccharomyces cerevisiae and Saccharomyces cerevisiae S288C. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
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

Phosphorylation patterns of the C-terminal domain (CTD) of largest subunit of RNA polymerase II (called the CTD code) orchestrate the recruitment of RNA processing and transcription factors. Recent studies showed that not only serines and tyrosines but also threonines of the CTD can be phosphorylated with a number of functional consequences, including the interaction with yeast transcription termination factor, Rtt103p. Here, we report the solution structure of the Rtt103p CTD-interacting domain (CID) bound to Thr4 phosphorylated CTD, a poorly understood letter of the CTD code. The structure reveals a direct recognition of the phospho-Thr4 mark by Rtt103p CID and extensive interactions involving residues from three repeats of the CTD heptad. Intriguingly, Rtt103p's CID binds equally well Thr4 and Ser2 phosphorylated CTD A doubly phosphorylated CTD at Ser2 and Thr4 diminishes its binding affinity due to electrostatic repulsion. Our structural data suggest that the recruitment of a CID-containing CTD-binding factor may be coded by more than one letter of the CTD code.

Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p.,Jasnovidova O, Krejcikova M, Kubicek K, Stefl R EMBO Rep. 2017 May 2. pii: e201643723. doi: 10.15252/embr.201643723. PMID:28468956^[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, Krejcikova M, Kubicek K, Stefl R. Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p. EMBO Rep. 2017 May 2. pii: e201643723. doi: 10.15252/embr.201643723. PMID:28468956 doi:http://dx.doi.org/10.15252/embr.201643723

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/5lvf"

@@ Line 1: / Line 1: @@
 ==Solution structure of Rtt103 CTD-interacting domain bound to a Thr4 phosphorylated CTD peptide==
-<StructureSection load='5lvf' size='340' side='right'caption='[[5lvf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='5lvf' size='340' side='right'caption='[[5lvf]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lvf]] 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=5LVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LVF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lvf]] 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=5LVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LVF FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=TPO:PHOSPHOTHREONINE'>TPO</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=5lvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvf OCA], [http://pdbe.org/5lvf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lvf RCSB], [http://www.ebi.ac.uk/pdbsum/5lvf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvf 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=5lvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvf OCA], [https://pdbe.org/5lvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lvf RCSB], [https://www.ebi.ac.uk/pdbsum/5lvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvf 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]]
-[[Category: Krejcikova, M]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Kubicek, K]]
+[[Category: Jasnovidova O]]
-[[Category: Stefl, R]]
+[[Category: Krejcikova M]]
-[[Category: Ctd-interacting domain]]
+[[Category: Kubicek K]]
-[[Category: Rnapii ctd]]
+[[Category: Stefl R]]
-[[Category: Transcription]]

5lvf

From Proteopedia

Revision as of 18:51, 18 October 2023

Solution structure of Rtt103 CTD-interacting domain bound to a Thr4 phosphorylated CTD peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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