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8FNI

Cryo-EM structure of RNase-treated RESC-B in trypanosomal RNA editing

This is a non-PDB format compatible entry.
Summary for 8FNI
Entry DOI10.2210/pdb8fni/pdb
EMDB information29314
DescriptormRNA, RNA-editing substrate-binding complex protein 13 (RESC13), RNA-editing substrate-binding complex protein 14 (RESC14), ... (11 entities in total)
Functional Keywordsheat repeat, trypanosoma, rna editing substrate binding complex, grna, rna binding protein-rna complex, rna binding protein/rna
Biological sourceTrypanosoma brucei
More
Total number of polymer chains11
Total formula weight527259.70
Authors
Primary citationLiu, S.,Wang, H.,Li, X.,Zhang, F.,Lee, J.K.J.,Li, Z.,Yu, C.,Hu, J.J.,Zhao, X.,Suematsu, T.,Alvarez-Cabrera, A.L.,Liu, Q.,Zhang, L.,Huang, L.,Aphasizheva, I.,Aphasizhev, R.,Zhou, Z.H.
Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing.
Science, 381:eadg4725-eadg4725, 2023
Cited by
PubMed Abstract: In , the editosome, composed of RNA-editing substrate-binding complex (RESC) and RNA-editing catalytic complex (RECC), orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs (mRNAs). The mechanism of information transfer from gRNA to mRNA is unclear owing to a lack of high-resolution structures for these complexes. With cryo-electron microscopy and functional studies, we have captured gRNA-stabilizing RESC-A and gRNA-mRNA-binding RESC-B and RESC-C particles. RESC-A sequesters gRNA termini, thus promoting hairpin formation and blocking mRNA access. The conversion of RESC-A into RESC-B or -C unfolds gRNA and allows mRNA selection. The ensuing gRNA-mRNA duplex protrudes from RESC-B, likely exposing editing sites to RECC-catalyzed cleavage, uridine insertion or deletion, and ligation. Our work reveals a remodeling event facilitating gRNA-mRNA hybridization and assembly of a macromolecular substrate for the editosome's catalytic modality.
PubMed: 37410820
DOI: 10.1126/science.adg4725
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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