2x1a: Difference between revisions

Latest revision as of 10:19, 9 May 2024

Structure of Rna15 RRM with RNA bound (G)

Structural highlights

2x1a is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.05Å
Ligands:	MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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:https://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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OCA

[1] 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

[2] 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:https://dx.doi.org/10.1073/pnas.101046598

[3] 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

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='2x1a' size='340' side='right'caption='[[2x1a]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x1a]] is a 2 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=2X1A OCA]. For a <b>guided tour on the structure components</b> use [https://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]] 2.05&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2x1b|2x1b]], [[2x1f|2x1f]]</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=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>
+== 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[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]]

2x1a: Difference between revisions

Latest revision as of 10:19, 9 May 2024

Structure of Rna15 RRM with RNA bound (G)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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