3riu: Difference between revisions
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==Crystal structure of Drosophila hexameric C3PO formed by truncated Translin and Trax== | |||
=== | <StructureSection load='3riu' size='340' side='right' caption='[[3riu]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3riu]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RIU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RIU FirstGlance]. <br> | |||
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG11761, Dmel_CG11761, translin, trsn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]), Dmel_CG5063, Trax ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</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=3riu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3riu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3riu RCSB], [http://www.ebi.ac.uk/pdbsum/3riu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Trax-translin heteromers, also known as C3PO, have been proposed to activate the RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand. We report on the crystal structure of hexameric Drosophila C3PO formed by truncated translin and Trax, along with electron microscopic and mass spectrometric studies on octameric C3PO formed by full-length translin and Trax. Our studies establish that Trax adopts the translin fold, possesses catalytic centers essential for C3PO's endoRNase activity and interacts extensively with translin to form an octameric assembly. The catalytic pockets of Trax subunits are located within the interior chamber of the octameric scaffold. Truncated C3PO, like full-length C3PO, shows endoRNase activity that leaves 3'-hydroxyl-cleaved ends. We have measured the catalytic activity of C3PO and shown it to cleave almost stoichiometric amounts of substrate per second. | |||
Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex.,Tian Y, Simanshu DK, Ascano M, Diaz-Avalos R, Park AY, Juranek SA, Rice WJ, Yin Q, Robinson CV, Tuschl T, Patel DJ Nat Struct Mol Biol. 2011 Jun;18(6):658-64. Epub 2011 May 8. PMID:21552261<ref>PMID:21552261</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Patel, D J | [[Category: Patel, D J]] | ||
[[Category: Simanshu, D K | [[Category: Simanshu, D K]] | ||
[[Category: Tian, Y | [[Category: Tian, Y]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Nucleus]] | [[Category: Nucleus]] | ||
Revision as of 14:09, 19 December 2014
Crystal structure of Drosophila hexameric C3PO formed by truncated Translin and TraxCrystal structure of Drosophila hexameric C3PO formed by truncated Translin and Trax
Structural highlights
Publication Abstract from PubMedTrax-translin heteromers, also known as C3PO, have been proposed to activate the RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand. We report on the crystal structure of hexameric Drosophila C3PO formed by truncated translin and Trax, along with electron microscopic and mass spectrometric studies on octameric C3PO formed by full-length translin and Trax. Our studies establish that Trax adopts the translin fold, possesses catalytic centers essential for C3PO's endoRNase activity and interacts extensively with translin to form an octameric assembly. The catalytic pockets of Trax subunits are located within the interior chamber of the octameric scaffold. Truncated C3PO, like full-length C3PO, shows endoRNase activity that leaves 3'-hydroxyl-cleaved ends. We have measured the catalytic activity of C3PO and shown it to cleave almost stoichiometric amounts of substrate per second. Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex.,Tian Y, Simanshu DK, Ascano M, Diaz-Avalos R, Park AY, Juranek SA, Rice WJ, Yin Q, Robinson CV, Tuschl T, Patel DJ Nat Struct Mol Biol. 2011 Jun;18(6):658-64. Epub 2011 May 8. PMID:21552261[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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