4bru: Difference between revisions
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==Crystal structure of the yeast Dhh1-Edc3 complex== | |||
=== | <StructureSection load='4bru' size='340' side='right' caption='[[4bru]], [[Resolution|resolution]] 3.25Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bru]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BRU FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4brw|4brw]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></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=4bru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bru OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bru RCSB], [http://www.ebi.ac.uk/pdbsum/4bru PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/DHH1_YEAST DHH1_YEAST]] ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export. Required for sporulation.<ref>PMID:9504907</ref> <ref>PMID:11780629</ref> <ref>PMID:12032091</ref> <ref>PMID:11696541</ref> <ref>PMID:12930949</ref> <ref>PMID:12730603</ref> <ref>PMID:15166134</ref> <ref>PMID:15703442</ref> <ref>PMID:15706350</ref> [[http://www.uniprot.org/uniprot/EDC3_YEAST EDC3_YEAST]] Stimulates decapping of both stable and unstable mRNA during mRNA decay. Does not affect nonsense-mediated mRNA decay. Required for normal P-body assembly.<ref>PMID:18678652</ref> <ref>PMID:15020463</ref> | [[http://www.uniprot.org/uniprot/DHH1_YEAST DHH1_YEAST]] ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export. Required for sporulation.<ref>PMID:9504907</ref> <ref>PMID:11780629</ref> <ref>PMID:12032091</ref> <ref>PMID:11696541</ref> <ref>PMID:12930949</ref> <ref>PMID:12730603</ref> <ref>PMID:15166134</ref> <ref>PMID:15703442</ref> <ref>PMID:15706350</ref> [[http://www.uniprot.org/uniprot/EDC3_YEAST EDC3_YEAST]] Stimulates decapping of both stable and unstable mRNA during mRNA decay. Does not affect nonsense-mediated mRNA decay. Required for normal P-body assembly.<ref>PMID:18678652</ref> <ref>PMID:15020463</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Translational repression and deadenylation of eukaryotic mRNAs result either in the sequestration of the transcripts in a nontranslatable pool or in their degradation. Removal of the 5' cap structure is a crucial step that commits deadenylated mRNAs to 5'-to-3' degradation. Pat1, Edc3 and the DEAD-box protein Dhh1 are evolutionary conserved factors known to participate in both translational repression and decapping, but their interplay is currently unclear. We report the 2.8 A resolution structure of yeast Dhh1 bound to the N-terminal domain of Pat1. The structure shows how Pat1 wraps around the C-terminal RecA domain of Dhh1, docking onto the Phe-Asp-Phe (FDF) binding site. The FDF-binding site of Dhh1 also recognizes Edc3, revealing why the binding of Pat1 and Edc3 on Dhh1 are mutually exclusive events. Using co-immunoprecipitation assays and structure-based mutants, we demonstrate that the mode of Dhh1-Pat1 recognition is conserved in humans. Pat1 and Edc3 also interfere and compete with the RNA-binding properties of Dhh1. Mapping the RNA-binding sites on Dhh1 with a crosslinking-mass spectrometry approach shows a large RNA-binding surface around the C-terminal RecA domain, including the FDF-binding pocket. The results suggest a model for how Dhh1-containing messenger ribonucleoprotein particles might be remodeled upon Pat1 and Edc3 binding. | |||
Structural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactions.,Sharif H, Ozgur S, Sharma K, Basquin C, Urlaub H, Conti E Nucleic Acids Res. 2013 Jul 12. PMID:23851565<ref>PMID:23851565</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: RNA helicase]] | [[Category: RNA helicase]] | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
[[Category: Basquin, C | [[Category: Basquin, C]] | ||
[[Category: Conti, E | [[Category: Conti, E]] | ||
[[Category: Ozgur, S | [[Category: Ozgur, S]] | ||
[[Category: Sharif, H | [[Category: Sharif, H]] | ||
[[Category: Sharma, K | [[Category: Sharma, K]] | ||
[[Category: Urlaub, H | [[Category: Urlaub, H]] | ||
[[Category: Dead-box]] | [[Category: Dead-box]] | ||
[[Category: Decapping]] | [[Category: Decapping]] | ||
