4brw
From Proteopedia
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| - | + | ==Crystal structure of the yeast Dhh1-Pat1 complex== | |
| - | + | <StructureSection load='4brw' size='340' side='right' caption='[[4brw]], [[Resolution|resolution]] 2.79Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4brw]] 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=4BRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BRW FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bru|4bru]]</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=4brw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4brw RCSB], [http://www.ebi.ac.uk/pdbsum/4brw 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/PAT1_YEAST PAT1_YEAST]] Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.<ref>PMID:8816497</ref> <ref>PMID:8972867</ref> <ref>PMID:10523645</ref> <ref>PMID:10394921</ref> <ref>PMID:10747033</ref> <ref>PMID:10779343</ref> <ref>PMID:10913177</ref> <ref>PMID:11027264</ref> <ref>PMID:10761922</ref> <ref>PMID:11514438</ref> <ref>PMID:12773554</ref> <ref>PMID:16179257</ref> <ref>PMID:17875743</ref> <ref>PMID:17429074</ref> <ref>PMID:17513695</ref> <ref>PMID:18086885</ref> <ref>PMID:19901074</ref> <ref>PMID:20832728</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/PAT1_YEAST PAT1_YEAST]] Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.<ref>PMID:8816497</ref> <ref>PMID:8972867</ref> <ref>PMID:10523645</ref> <ref>PMID:10394921</ref> <ref>PMID:10747033</ref> <ref>PMID:10779343</ref> <ref>PMID:10913177</ref> <ref>PMID:11027264</ref> <ref>PMID:10761922</ref> <ref>PMID:11514438</ref> <ref>PMID:12773554</ref> <ref>PMID:16179257</ref> <ref>PMID:17875743</ref> <ref>PMID:17429074</ref> <ref>PMID:17513695</ref> <ref>PMID:18086885</ref> <ref>PMID:19901074</ref> <ref>PMID:20832728</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: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mrnp remodeling]] | [[Category: Mrnp remodeling]] | ||
[[Category: P- bod]] | [[Category: P- bod]] | ||
[[Category: Translational repression]] | [[Category: Translational repression]] | ||
Revision as of 18:57, 25 December 2014
Crystal structure of the yeast Dhh1-Pat1 complex
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