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| | <StructureSection load='2x1a' size='340' side='right'caption='[[2x1a]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='2x1a' size='340' side='right'caption='[[2x1a]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x1a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X1A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x1a]] is a 2 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=2X1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X1A 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]] 2.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x1b|2x1b]], [[2x1f|2x1f]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=2x1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1a OCA], [http://pdbe.org/2x1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x1a RCSB], [http://www.ebi.ac.uk/pdbsum/2x1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1a 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=2x1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1a OCA], [https://pdbe.org/2x1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x1a RCSB], [https://www.ebi.ac.uk/pdbsum/2x1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RNA15_YEAST RNA15_YEAST] RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.<ref>PMID:7992054</ref> <ref>PMID:11344258</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Goldstone, D C]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Pancevac, C]] | + | [[Category: Goldstone DC]] |
| - | [[Category: Ramos, A]] | + | [[Category: Pancevac C]] |
| - | [[Category: Taylor, I A]] | + | [[Category: Ramos A]] |
| - | [[Category: Mrna processing]] | + | [[Category: Taylor IA]] |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Transcription-rna complex]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
RNA15_YEAST RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.[1] [2]
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
Rna15 is a core subunit of cleavage factor IA (CFIA), an essential transcriptional 3'-end processing factor from Saccharomyces cerevisiae. CFIA is required for polyA site selection/cleavage targeting RNA sequences that surround polyadenylation sites in the 3'-UTR of RNA polymerase-II transcripts. RNA recognition by CFIA is mediated by an RNA recognition motif (RRM) contained in the Rna15 subunit of the complex. We show here that Rna15 has a strong and unexpected preference for GU containing RNAs and reveal the molecular basis for a base selectivity mechanism that accommodates G or U but discriminates against C and A bases. This mode of base selectivity is rather different to that observed in other RRM-RNA structures and is structurally conserved in CstF64, the mammalian counterpart of Rna15. Our observations provide evidence for a highly conserved mechanism of base recognition amongst the 3'-end processing complexes that interact with the U-rich or U/G-rich elements at 3'-end cleavage/polyadenylation sites.
Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3'-end processing factors.,Pancevac C, Goldstone DC, Ramos A, Taylor IA Nucleic Acids Res. 2010 May;38(9):3119-32. Epub 2010 Jan 21. PMID:20097654[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Minvielle-Sebastia L, Preker PJ, Keller W. RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor. Science. 1994 Dec 9;266(5191):1702-5. PMID:7992054
- ↑ Gross S, Moore C. Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6080-5. Epub 2001 May 8. PMID:11344258 doi:http://dx.doi.org/10.1073/pnas.101046598
- ↑ Pancevac C, Goldstone DC, Ramos A, Taylor IA. Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3'-end processing factors. Nucleic Acids Res. 2010 May;38(9):3119-32. Epub 2010 Jan 21. PMID:20097654 doi:10.1093/nar/gkq002
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