9F67
Trypanosoma brucei nuclear cap-binding complex (CBC) bound to cap4
This is a non-PDB format compatible entry.
Summary for 9F67
| Entry DOI | 10.2210/pdb9f67/pdb |
| EMDB information | 50217 |
| Descriptor | Nuclear cap binding complex subunit CBP30, Nuclear cap binding complex subunit CBP110, Nuclear cap-binding protein subunit 2, ... (4 entities in total) |
| Functional Keywords | nuclear cap binding complex, cap-4, rna binding protein |
| Biological source | Trypanosoma brucei brucei More |
| Total number of polymer chains | 4 |
| Total formula weight | 165963.99 |
| Authors | Bernhard, H.,Warminski, M.,Dolce, L.G.,Kowalinski, E. (deposition date: 2024-04-30, release date: 2024-12-25, Last modification date: 2025-01-29) |
| Primary citation | Bernhard, H.,Petrzilkova, H.,Popelarova, B.,Ziemkiewicz, K.,Bartosik, K.,Warminski, M.,Tengo, L.,Groger, H.,Dolce, L.G.,Mackereth, C.D.,Micura, R.,Jemielity, J.,Kowalinski, E. Structural basis of Spliced Leader RNA recognition by the Trypanosoma brucei cap-binding complex. Nat Commun, 16:685-685, 2025 Cited by PubMed Abstract: Kinetoplastids are a clade of eukaryotic protozoans that include human parasitic pathogens like trypanosomes and Leishmania species. In these organisms, protein-coding genes are transcribed as polycistronic pre-mRNAs, which need to be processed by the coupled action of trans-splicing and polyadenylation to yield monogenic mature mRNAs. During trans-splicing, a universal RNA sequence, the spliced leader RNA (SL RNA) mini-exon, is added to the 5'-end of each mRNA. The 5'-end of this mini-exon carries a hypermethylated cap structure and is bound by a trypanosomatid-specific cap-binding complex (CBC). The function of three of the kinetoplastid CBC subunits is unknown, but an essential role in cap-binding and trans-splicing has been suggested. Here, we report cryo-EM structures that reveal the molecular architecture of the Trypanosoma brucei CBC (TbCBC) complex. We find that TbCBC interacts with two distinct features of the SL RNA. The TbCBP20 subunit interacts with the mG cap while TbCBP66 recognizes double-stranded portions of the SL RNA. Our findings pave the way for future research on mRNA maturation in kinetoplastids. Moreover, the observed structural similarities and differences between TbCBC and the mammalian cap-binding complex will be crucial for considering the potential of TbCBC as a target for anti-trypanosomatid drug development. PubMed: 39814716DOI: 10.1038/s41467-024-55373-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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