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| | <StructureSection load='6j9r' size='340' side='right'caption='[[6j9r]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6j9r' size='340' side='right'caption='[[6j9r]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j9r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster_american_nodavirus_(anv)_sw-2009a Drosophila melanogaster american nodavirus (anv) sw-2009a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J9R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J9R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j9r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster_American_nodavirus_(ANV)_SW-2009a Drosophila melanogaster American nodavirus (ANV) SW-2009a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J9R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=6j9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j9r OCA], [http://pdbe.org/6j9r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j9r RCSB], [http://www.ebi.ac.uk/pdbsum/6j9r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j9r 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=6j9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j9r OCA], [https://pdbe.org/6j9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j9r RCSB], [https://www.ebi.ac.uk/pdbsum/6j9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j9r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BRAT_DROME BRAT_DROME]] Plays a central role in translation repression of hb mRNA by being recruited by nos and pum to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR. Probably recruited by other proteins to repress translation of other mRNAs in other tissues. Involved in the regulation of ribosomal RNA synthesis and cell growth. Participates in abdominal segmentation and imaginal disk development. Involved in brain tumor suppression, by acting as a growth suppressor in the larval brain.<ref>PMID:11274060</ref> <ref>PMID:11807032</ref> | + | [https://www.uniprot.org/uniprot/BRAT_DROME BRAT_DROME] Plays a central role in translation repression of hb mRNA by being recruited by nos and pum to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR. Probably recruited by other proteins to repress translation of other mRNAs in other tissues. Involved in the regulation of ribosomal RNA synthesis and cell growth. Participates in abdominal segmentation and imaginal disk development. Involved in brain tumor suppression, by acting as a growth suppressor in the larval brain.<ref>PMID:11274060</ref> <ref>PMID:11807032</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shan, Z]] | + | [[Category: Shan Z]] |
| - | [[Category: Wang, W]] | + | [[Category: Wang W]] |
| - | [[Category: Brat]]
| + | |
| - | [[Category: Coiled-coil domain]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translational repressor]]
| + | |
| - | [[Category: Trim]]
| + | |
| Structural highlights
Function
BRAT_DROME Plays a central role in translation repression of hb mRNA by being recruited by nos and pum to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR. Probably recruited by other proteins to repress translation of other mRNAs in other tissues. Involved in the regulation of ribosomal RNA synthesis and cell growth. Participates in abdominal segmentation and imaginal disk development. Involved in brain tumor suppression, by acting as a growth suppressor in the larval brain.[1] [2]
Publication Abstract from PubMed
Drosophila brain tumor (Brat) is a translational repressor belonging to the tripartite motif (TRIM) protein superfamily. During the asymmetric division of Drosophila neuroblasts, Brat localizes at the basal cortex via direct interaction with the scaffolding protein Miranda (Mira), and segregates into the basal ganglion mother cells after cell division. It was previously reported that both the coiled-coil (CC) and NHL domains of Brat are required for the interaction with Mira, but the underlying structural basis is elusive. Here, we determine the crystal structure of Brat-CC domain (aa 376-511) at 2.5 A, showing that Brat-CC forms an elongated antiparallel dimer through an unconventional CC structure. The dimeric assembly in Brat-CC structure is similar to its counterparts in other TRIM proteins, but Brat-CC also exhibits some distinct structural features. We also demonstrate that the CC domain could not bind Mira by its own, neither does the isolated NHL domain of Brat. Rather, Brat binds to Mira through the CC-NHL domain tandem, indicating that the function of the CC domain is to assemble Brat-NHL in dimeric form, which is necessary for Mira binding.
Crystal structure of the coiled-coil domain of Drosophila TRIM protein Brat.,Liu C, Shan Z, Diao J, Wen W, Wang W Proteins. 2019 Apr 8. doi: 10.1002/prot.25691. PMID:30958583[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sonoda J, Wharton RP. Drosophila Brain Tumor is a translational repressor. Genes Dev. 2001 Mar 15;15(6):762-73. PMID:11274060 doi:http://dx.doi.org/10.1101/gad.870801
- ↑ Frank DJ, Edgar BA, Roth MB. The Drosophila melanogaster gene brain tumor negatively regulates cell growth and ribosomal RNA synthesis. Development. 2002 Jan;129(2):399-407. PMID:11807032
- ↑ Liu C, Shan Z, Diao J, Wen W, Wang W. Crystal structure of the coiled-coil domain of Drosophila TRIM protein Brat. Proteins. 2019 Apr 8. doi: 10.1002/prot.25691. PMID:30958583 doi:http://dx.doi.org/10.1002/prot.25691
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