Summary for 8CDP
| Entry DOI | 10.2210/pdb8cdp/pdb |
| EMDB information | 16592 |
| Descriptor | Guide_RNA_associated_protein_-_putative, Mitochondrial guide RNA binding complex subunit 2 (2 entities in total) |
| Functional Keywords | resc, rna editing, cryo-em structure, trypanosoma brucei, rna binding protein |
| Biological source | Trypanosoma brucei brucei More |
| Total number of polymer chains | 2 |
| Total formula weight | 104934.77 |
| Authors | Dolce, L.G.,Weis, F.,Kowalinski, E. (deposition date: 2023-01-31, release date: 2023-03-29, Last modification date: 2024-07-24) |
| Primary citation | Dolce, L.G.,Nesterenko, Y.,Walther, L.,Weis, F.,Kowalinski, E. Structural basis for guide RNA selection by the RESC1-RESC2 complex. Nucleic Acids Res., 51:4602-4612, 2023 Cited by PubMed Abstract: Kinetoplastid parasites, such as trypanosomes or leishmania, rely on RNA-templated RNA editing to mature mitochondrial cryptic pre-mRNAs into functional protein-coding transcripts. Processive pan-editing of multiple editing blocks within a single transcript is dependent on the 20-subunit RNA editing substrate binding complex (RESC) that serves as a platform to orchestrate the interactions between pre-mRNA, guide RNAs (gRNAs), the catalytic RNA editing complex (RECC), and a set of RNA helicases. Due to the lack of molecular structures and biochemical studies with purified components, neither the spacio-temporal interplay of these factors nor the selection mechanism for the different RNA components is understood. Here we report the cryo-EM structure of Trypanosoma brucei RESC1-RESC2, a central hub module of the RESC complex. The structure reveals that RESC1 and RESC2 form an obligatory domain-swapped dimer. Although the tertiary structures of both subunits closely resemble each other, only RESC2 selectively binds 5'-triphosphate-nucleosides, a defining characteristic of gRNAs. We therefore propose RESC2 as the protective 5'-end binding site for gRNAs within the RESC complex. Overall, our structure provides a starting point for the study of the assembly and function of larger RNA-bound kinetoplast RNA editing modules and might aid in the design of anti-parasite drugs. PubMed: 36999600DOI: 10.1093/nar/gkad217 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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