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4nut

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

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 ==Crystal structure of the complex between Snu13p and the PEP domain of Rsa1==
-<StructureSection load='4nut' size='340' side='right' caption='[[4nut]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='4nut' size='340' side='right'caption='[[4nut]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[4nut]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4NUT 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</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=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>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4nut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nut OCA], [https://pdbe.org/4nut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nut RCSB], [https://www.ebi.ac.uk/pdbsum/4nut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nut ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/SNU13_YEAST SNU13_YEAST] Common component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA. In association with box C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and site-specific 2'-O-methylation of substrate RNAs. Essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs.<ref>PMID:11081632</ref> <ref>PMID:12215523</ref> <ref>PMID:14730029</ref>
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Branlant, C]]
+[[Category: Large Structures]]
-[[Category: Chagot, M E]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Charpentier, B]]
+[[Category: Branlant C]]
-[[Category: Charron, C]]
+[[Category: Chagot ME]]
-[[Category: Manival, X]]
+[[Category: Charpentier B]]
-[[Category: Rna binding protein]]
+[[Category: Charron C]]
-[[Category: Snornp assembly]]
+[[Category: Manival X]]

4nut

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

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