6f9s
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the C-terminal RecA domain of DDX6 in complex with a conserved peptide from LSM14== | |
| + | <StructureSection load='6f9s' size='340' side='right' caption='[[6f9s]], [[Resolution|resolution]] 3.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6f9s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F9S FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6f9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f9s OCA], [http://pdbe.org/6f9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f9s RCSB], [http://www.ebi.ac.uk/pdbsum/6f9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f9s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN]] Note=A chromosomal aberration involving DDX6 may be a cause of hematopoietic tumors such as B-cell lymphomas. Translocation t(11;14)(q23;q32). | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN]] In the process of mRNA degradation, may play a role in mRNA decapping. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The LSM domain-containing protein LSM14/Rap55 plays a role in mRNA decapping, translational repression, and RNA granule (P-body) assembly. How LSM14 interacts with the mRNA silencing machinery, including the eIF4E-binding protein 4E-T and the DEAD-box helicase DDX6, is poorly understood. Here we report the crystal structure of the LSM domain of LSM14 bound to a highly conserved C-terminal fragment of 4E-T. The 4E-T C-terminus forms a bi-partite motif that wraps around the N-terminal LSM domain of LSM14. We also determined the crystal structure of LSM14 bound to the C-terminal RecA-like domain of DDX6. LSM14 binds DDX6 via a unique non-contiguous motif with distinct directionality as compared to other DDX6-interacting proteins. Together with mutational and proteomic studies, the LSM14-DDX6 structure reveals that LSM14 has adopted a divergent mode of binding DDX6 in order to support the formation of mRNA silencing complexes and P-body assembly. | ||
| - | + | Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.,Brandmann T, Fakim H, Padamsi Z, Youn JY, Gingras AC, Fabian MR, Jinek M EMBO J. 2018 Mar 6. pii: embj.201797869. doi: 10.15252/embj.201797869. PMID:29510985<ref>PMID:29510985</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6f9s" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: RNA helicase]] | ||
[[Category: Brandmann, T]] | [[Category: Brandmann, T]] | ||
| + | [[Category: Jinek, M]] | ||
| + | [[Category: Decapping]] | ||
| + | [[Category: Mrna turnover]] | ||
| + | [[Category: Rna]] | ||
| + | [[Category: Translational repression]] | ||
Revision as of 07:43, 21 March 2018
Crystal structure of the C-terminal RecA domain of DDX6 in complex with a conserved peptide from LSM14
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