8CDP

Cryo-EM structure of the RESC1-RESC2 complex

これはPDB形式変換不可エントリーです。

8CDP の概要

• エントリーDOI: 10.2210/pdb8cdp/pdb
• EMDBエントリー: 16592
• 分子名称: Guide_RNA_associated_protein_-_putative, Mitochondrial guide RNA binding complex subunit 2 (2 entities in total)
• 機能のキーワード: resc, rna editing, cryo-em structure, trypanosoma brucei, rna binding protein
• 由来する生物種: Trypanosoma brucei brucei; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104934.77

構造登録者

Dolce, L.G.,Weis, F.,Kowalinski, E. (登録日: 2023-01-31, 公開日: 2023-03-29, 最終更新日: 2025-07-09)

主引用文献

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

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: 36999600
DOI: 10.1093/nar/gkad217

実験手法

ELECTRON MICROSCOPY (3.4 Å)