2l0i

From Proteopedia

(Difference between revisions)

Revision as of 07:34, 14 April 2021

Solution structure of Rtt103 CTD-interacting domain bound to a Ser2 phosphorylated CTD peptide

Structural highlights

2l0i is a 2 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	2km4
Gene:	RTT103, YDR289C (ATCC 18824)
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]

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 PubMed

Phosphorylation 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

↑ 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
↑ Lunde BM, Reichow SL, Kim M, Suh H, Leeper TC, Yang F, Mutschler H, Buratowski S, Meinhart A, Varani G. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nat Struct Mol Biol. 2010 Oct;17(10):1195-201. Epub 2010 Sep 5. PMID:20818393 doi:10.1038/nsmb.1893

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l0i"

@@ Line 1: / Line 1: @@
 ==Solution structure of Rtt103 CTD-interacting domain bound to a Ser2 phosphorylated CTD peptide==
-<StructureSection load='2l0i' size='340' side='right' caption='[[2l0i]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2l0i' size='340' side='right'caption='[[2l0i]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l0i]] is a 2 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=2L0I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L0I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l0i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L0I 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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2km4|2km4]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2km4|2km4]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTT103, YDR289C ([https://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=2l0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0i OCA], [http://pdbe.org/2l0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l0i RCSB], [http://www.ebi.ac.uk/pdbsum/2l0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0i 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=2l0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0i OCA], [https://pdbe.org/2l0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0i RCSB], [https://www.ebi.ac.uk/pdbsum/2l0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0i 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[RNA polymerase|RNA polymerase]]
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Buratowski, S]]
 [[Category: Kim, M]]

2l0i

From Proteopedia

Revision as of 07:34, 14 April 2021

Solution structure of Rtt103 CTD-interacting domain bound to a Ser2 phosphorylated CTD peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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