2X1A
Structure of Rna15 RRM with RNA bound (G)
Summary for 2X1A
Entry DOI | 10.2210/pdb2x1a/pdb |
Related | 2X1B 2X1F |
Descriptor | MRNA 3'-END-PROCESSING PROTEIN RNA15, 5'-R(*GP*UP*UP*GP*UP)-3', MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | transcription-rna complex, translation, nucleus, rna-binding, mrna processing, transcription/rna |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
Cellular location | Nucleus: P25299 |
Total number of polymer chains | 2 |
Total formula weight | 12389.20 |
Authors | Pancevac, C.,Goldstone, D.C.,Ramos, A.,Taylor, I.A. (deposition date: 2010-01-06, release date: 2010-02-02, Last modification date: 2024-05-08) |
Primary citation | Pancevac, C.,Goldstone, D.C.,Ramos, A.,Taylor, I.A. Structure of the RNA15 Rrm-RNA Complex Reveals the Molecular Basis of Gu Specificity in Transcriptional 3-End Processing Factors. Nucleic Acids Res., 38:3119-, 2010 Cited by PubMed Abstract: 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. PubMed: 20097654DOI: 10.1093/NAR/GKQ002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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