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2nax

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Structure of CCHC zinc finger domain of Pcf11

Structural highlights

2nax is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PCF11_YEAST Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.^[1] ^[2]

Publication Abstract from PubMed

3'-end processing of pre-mRNAs prior to packaging and export to the cytoplasm of the mature transcript is a highly regulated process executed by several tens of protein factors that recognize poorly conserved RNA signals. Among them is Pcf11, a highly conserved, multi-domain protein that links transcriptional elongation, 3'-end processing and transcription termination. Here we report the structure and biochemical function of Pcf11's C-terminal domain, which is conserved from yeast to humans. We identify a novel zinc finger fold, resembling a trillium flower. Structural, biochemical and genetic analyses reveal a highly conserved surface that plays a critical role in both cleavage and polyadenylation. These findings provide further insight into this important protein and its multiple functional roles during co-transcriptional RNA processing.

The C-terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'- end processing.,Yang F, Hsu P, Lee SD, Yang W, Hoskinson D, Xu W, Moore C, Varani G RNA. 2016 Oct 25. pii: rna.058354.116. PMID:27780845^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gross S, Moore C. Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6080-5. Epub 2001 May 8. PMID:11344258 doi:http://dx.doi.org/10.1073/pnas.101046598
↑ Zhang Z, Fu J, Gilmour DS. CTD-dependent dismantling of the RNA polymerase II elongation complex by the pre-mRNA 3'-end processing factor, Pcf11. Genes Dev. 2005 Jul 1;19(13):1572-80. PMID:15998810 doi:http://dx.doi.org/19/13/1572
↑ Yang F, Hsu P, Lee SD, Yang W, Hoskinson D, Xu W, Moore C, Varani G. The C-terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'- end processing. RNA. 2016 Oct 25. pii: rna.058354.116. PMID:27780845 doi:http://dx.doi.org/10.1261/rna.058354.116

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/2nax"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Varani G | Yang F

@@ Line 1: / Line 1: @@
 ==Structure of CCHC zinc finger domain of Pcf11==
-<StructureSection load='2nax' size='340' side='right'caption='[[2nax]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2nax' size='340' side='right'caption='[[2nax]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2nax]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NAX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2NAX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2nax]] is a 1 chain structure with sequence from [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=2NAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NAX FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2nax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nax OCA], [http://pdbe.org/2nax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nax RCSB], [http://www.ebi.ac.uk/pdbsum/2nax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nax 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=2nax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nax OCA], [https://pdbe.org/2nax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nax RCSB], [https://www.ebi.ac.uk/pdbsum/2nax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nax ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PCF11_YEAST PCF11_YEAST]] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.<ref>PMID:11344258</ref> <ref>PMID:15998810</ref>
+[https://www.uniprot.org/uniprot/PCF11_YEAST PCF11_YEAST] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.<ref>PMID:11344258</ref> <ref>PMID:15998810</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Varani, G]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Yang, F]]
+[[Category: Varani G]]
-[[Category: Metal binding protein]]
+[[Category: Yang F]]
-[[Category: Zinc finger]]

2nax

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Current revision

Structure of CCHC zinc finger domain of Pcf11

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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