4nut

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'''Unreleased structure'''
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==Crystal structure of the complex between Snu13p and the PEP domain of Rsa1==
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<StructureSection load='4nut' size='340' side='right' caption='[[4nut]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4nut]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NUT FirstGlance]. <br>
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</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>
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<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=4nut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nut RCSB], [http://www.ebi.ac.uk/pdbsum/4nut PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In vitro, assembly of box C/D small nucleolar ribonucleoproteins (snoRNPs) involves the sequential recruitment of core proteins to snoRNAs. In vivo, however, assembly factors are required (NUFIP, BCD1, and the HSP90-R2TP complex), and it is unknown whether a similar sequential scheme applies. In this paper, we describe systematic quantitative stable isotope labeling by amino acids in cell culture proteomic experiments and the crystal structure of the core protein Snu13p/15.5K bound to a fragment of the assembly factor Rsa1p/NUFIP. This revealed several unexpected features: (a) the existence of a protein-only pre-snoRNP complex containing five assembly factors and two core proteins, 15.5K and Nop58; (b) the characterization of ZNHIT3, which is present in the protein-only complex but gets released upon binding to C/D snoRNAs; (c) the dynamics of the R2TP complex, which appears to load/unload RuvBL AAA+ adenosine triphosphatase from pre-snoRNPs; and (d) a potential mechanism for preventing premature activation of snoRNP catalytic activity. These data provide a framework for understanding the assembly of box C/D snoRNPs.
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The entry 4nut is ON HOLD until Paper Publication
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Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control.,Bizarro J, Charron C, Boulon S, Westman B, Pradet-Balade B, Vandermoere F, Chagot ME, Hallais M, Ahmad Y, Leonhardt H, Lamond A, Manival X, Branlant C, Charpentier B, Verheggen C, Bertrand E J Cell Biol. 2014 Nov 24;207(4):463-480. Epub 2014 Nov 17. PMID:25404746<ref>PMID:25404746</ref>
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Authors: Charron, C., Chagot, M.E., Manival, X., Branlant, C., Charpentier, B.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of the complex between Snu13p and the PEP domain of Rsa1
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Branlant, C]]
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[[Category: Chagot, M E]]
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[[Category: Charpentier, B]]
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[[Category: Charron, C]]
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[[Category: Manival, X]]
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[[Category: Rna binding protein]]
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[[Category: Snornp assembly]]

Revision as of 16:08, 10 December 2014

Crystal structure of the complex between Snu13p and the PEP domain of Rsa1

4nut, resolution 1.55Å

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