1oo0: Difference between revisions

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<StructureSection load='1oo0' size='340' side='right'caption='[[1oo0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1oo0' size='340' side='right'caption='[[1oo0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oo0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OO0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oo0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OO0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAGO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), TSU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oo0 OCA], [http://pdbe.org/1oo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oo0 RCSB], [http://www.ebi.ac.uk/pdbsum/1oo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oo0 ProSAT]</span></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=1oo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oo0 OCA], [https://pdbe.org/1oo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oo0 RCSB], [https://www.ebi.ac.uk/pdbsum/1oo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oo0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MGN_DROME MGN_DROME]] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.<ref>PMID:8026338</ref> <ref>PMID:9272960</ref> <ref>PMID:9210377</ref> <ref>PMID:12730685</ref> [[http://www.uniprot.org/uniprot/RBM8A_DROME RBM8A_DROME]] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.<ref>PMID:11691839</ref> <ref>PMID:12730685</ref> 
[https://www.uniprot.org/uniprot/MGN_DROME MGN_DROME] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.<ref>PMID:8026338</ref> <ref>PMID:9272960</ref> <ref>PMID:9210377</ref> <ref>PMID:12730685</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oo0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oo0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pre-mRNA splicing is essential for generating mature mRNA and is also important for subsequent mRNA export and quality control. The splicing history is imprinted on spliced mRNA through the deposition of a splicing-dependent multiprotein complex, the exon junction complex (EJC), at approximately 20 nucleotides upstream of exon-exon junctions. The EJC is a dynamic structure containing proteins functioning in the nuclear export and nonsense-mediated decay of spliced mRNAs. Mago nashi (Mago) and Y14 are core components of the EJC, and they form a stable heterodimer that strongly associates with spliced mRNA. Here we report a 1.85 A-resolution structure of the Drosophila Mago-Y14 complex. Surprisingly, the structure shows that the canonical RNA-binding surface of the Y14 RNA recognition motif (RRM) is involved in extensive protein-protein interactions with Mago. This unexpected finding provides important insights for understanding the molecular mechanisms of EJC assembly and RRM-mediated protein-protein interactions.
Crystal structure of the Drosophila Mago nashi-Y14 complex.,Shi H, Xu RM Genes Dev. 2003 Apr 15;17(8):971-6. PMID:12704080<ref>PMID:12704080</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oo0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Shi, H]]
[[Category: Shi H]]
[[Category: Xu, R M]]
[[Category: Xu RM]]
[[Category: Exon junction complex]]
[[Category: Protein complex]]
[[Category: Rna recognition motif]]
[[Category: Signaling protein]]
[[Category: Splicing]]

Latest revision as of 08:02, 14 February 2024

Crystal structure of the Drosophila Mago nashi-Y14 complex

1oo0, resolution 1.85Å

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