4brw
From Proteopedia
(Difference between revisions)
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<StructureSection load='4brw' size='340' side='right'caption='[[4brw]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='4brw' size='340' side='right'caption='[[4brw]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4brw]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4brw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4BRW FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bru|4bru]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4brw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brw OCA], [https://pdbe.org/4brw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4brw RCSB], [https://www.ebi.ac.uk/pdbsum/4brw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4brw ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://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> [[https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
| - | *[[Helicase|Helicase]] | + | *[[Helicase 3D structures|Helicase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:23, 31 August 2022
Crystal structure of the yeast Dhh1-Pat1 complex
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