View source for 4wzw


==Crystal structure of human Puf-A in complex with DNA==
<StructureSection load='4wzw' size='340' side='right'caption='[[4wzw]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wzw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9516&#8491;</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=4wzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzw OCA], [https://pdbe.org/4wzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzw RCSB], [https://www.ebi.ac.uk/pdbsum/4wzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PUM3_HUMAN PUM3_HUMAN] Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence specificity (PubMed:25512524). Involved in development of the eye and of primordial germ cells (By similarity).[UniProtKB:X1WGX5]<ref>PMID:21266351</ref> <ref>PMID:25512524</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pumilio/feminization of XX and XO animals (fem)-3 mRNA-binding factor (PUF) proteins bind sequence specifically to mRNA targets using a single-stranded RNA-binding domain comprising eight Pumilio (PUM) repeats. PUM repeats have now been identified in proteins that function in pre-rRNA processing, including human Puf-A and yeast Puf6. This is a role not previously ascribed to PUF proteins. Here we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an "L"-like shape. In contrast to classical PUF proteins, Puf-A forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues. We demonstrate that equivalent basic residues in yeast Puf6 are important for RNA binding, pre-rRNA processing, and mRNA localization. Thus, PUM repeats can be assembled into alternative folds that bind to structured nucleic acids in addition to forming canonical eight-repeat crescent-shaped RNA-binding domains found in classical PUF proteins.

A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.,Qiu C, McCann KL, Wine RN, Baserga SJ, Hall TM Proc Natl Acad Sci U S A. 2014 Dec 15. pii: 201407634. PMID:25512524<ref>PMID:25512524</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wzw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Hall TMT]]
[[Category: Qiu C]]