|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2ale' size='340' side='right'caption='[[2ale]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2ale' size='340' side='right'caption='[[2ale]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ale]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ale]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e7k|1e7k]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ale OCA], [https://pdbe.org/2ale PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ale RCSB], [https://www.ebi.ac.uk/pdbsum/2ale PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ale 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=2ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ale OCA], [https://pdbe.org/2ale PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ale RCSB], [https://www.ebi.ac.uk/pdbsum/2ale PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ale ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bella, J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Dobbyn, H C]] | + | [[Category: Bella J]] |
| - | [[Category: Keefe, R T.O]] | + | [[Category: Dobbyn HC]] |
| - | [[Category: McEwan, P A]] | + | [[Category: McEwan PA]] |
| - | [[Category: His-tag]] | + | [[Category: O'Keefe RT]] |
| - | [[Category: Rna]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Splicing]]
| + | |
| - | [[Category: Yeast]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Snu13p is a Saccharomyces cerevisiae protein essential for pre-messenger RNA splicing and pre-ribosomal RNA processing. Snu13p binds U4 snRNA of the spliceosome and box C/D snoRNAs of the pre-ribosomal RNA processing machinery to induce assembly of each ribonucleoprotein complex. Here, we present structural and biochemical analysis of Snu13p. The crystal structure of Snu13p reveals a region of the protein which could be important for protein interaction during ribonucleoprotein assembly. Using the structure of Snu13p we have designed the first temperature-sensitive mutants in Snu13p, L67W and I102A. Wild-type and mutant Snu13p proteins were assayed for binding to U4 snRNA and U3 snoRNA. Both temperature-sensitive mutants displayed significantly reduced RNA binding compared to wild-type protein. As the temperature-sensitive mutations are not in the known RNA binding region of Snu13p this indicates that these mutants indirectly influence the RNA binding properties of Snu13p. This work provides insight into Snu13p function during ribonucleoprotein assembly.
Analysis of pre-mRNA and pre-rRNA processing factor Snu13p structure and mutants.,Dobbyn HC, McEwan PA, Krause A, Novak-Frazer L, Bella J, O'Keefe RT Biochem Biophys Res Commun. 2007 Sep 7;360(4):857-62. Epub 2007 Jul 9. PMID:17631273[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Watkins NJ, Segault V, Charpentier B, Nottrott S, Fabrizio P, Bachi A, Wilm M, Rosbash M, Branlant C, Luhrmann R. A common core RNP structure shared between the small nucleoar box C/D RNPs and the spliceosomal U4 snRNP. Cell. 2000 Oct 27;103(3):457-66. PMID:11081632
- ↑ Galardi S, Fatica A, Bachi A, Scaloni A, Presutti C, Bozzoni I. Purified box C/D snoRNPs are able to reproduce site-specific 2'-O-methylation of target RNA in vitro. Mol Cell Biol. 2002 Oct;22(19):6663-8. PMID:12215523
- ↑ Dobbyn HC, O'Keefe RT. Analysis of Snu13p mutations reveals differential interactions with the U4 snRNA and U3 snoRNA. RNA. 2004 Feb;10(2):308-20. PMID:14730029
- ↑ Dobbyn HC, McEwan PA, Krause A, Novak-Frazer L, Bella J, O'Keefe RT. Analysis of pre-mRNA and pre-rRNA processing factor Snu13p structure and mutants. Biochem Biophys Res Commun. 2007 Sep 7;360(4):857-62. Epub 2007 Jul 9. PMID:17631273 doi:10.1016/j.bbrc.2007.06.163
|