View source for 2y35


==Crystal structure of Xrn1-substrate complex==
<StructureSection load='2y35' size='340' side='right'caption='[[2y35]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2y35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] 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=2Y35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y35 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2y35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y35 OCA], [https://pdbe.org/2y35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y35 RCSB], [https://www.ebi.ac.uk/pdbsum/2y35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y35 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E1JJR3_DROME E1JJR3_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Messenger RNA decay plays a central role in the regulation and surveillance of eukaryotic gene expression. The conserved multidomain exoribonuclease Xrn1 targets cytoplasmic RNA substrates marked by a 5' monophosphate for processive 5'-to-3' degradation by an unknown mechanism. Here, we report the crystal structure of an Xrn1-substrate complex. The single-stranded substrate is held in place by stacking of the 5'-terminal trinucleotide between aromatic side chains while a highly basic pocket specifically recognizes the 5' phosphate. Mutations of residues involved in binding the 5'-terminal nucleotide impair Xrn1 processivity. The substrate recognition mechanism allows Xrn1 to couple processive hydrolysis to duplex melting in RNA substrates with sufficiently long single-stranded 5' overhangs. The Xrn1-substrate complex structure thus rationalizes the exclusive specificity of Xrn1 for 5'-monophosphorylated substrates, ensuring fidelity of mRNA turnover, and posits a model for translocation-coupled unwinding of structured RNA substrates.

Coupled 5' nucleotide recognition and processivity in xrn1-mediated mRNA decay.,Jinek M, Coyle SM, Doudna JA Mol Cell. 2011 Mar 4;41(5):600-8. PMID:21362555<ref>PMID:21362555</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2y35" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Coyle SM]]
[[Category: Doudna JA]]
[[Category: Jinek M]]