View source for 2nax


==Structure of CCHC zinc finger domain of Pcf11==
<StructureSection load='2nax' size='340' side='right'caption='[[2nax]]' scene=''>
== Structural highlights ==
<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'>[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 ==
[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 ==
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<ref>PMID:27780845</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2nax" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Varani G]]
[[Category: Yang F]]