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9YFM

insect H/ACA snoRNP class II composite

This is a non-PDB format compatible entry.
Summary for 9YFM
Entry DOI10.2210/pdb9yfm/pdb
EMDB information72898
DescriptorH/ACA ribonucleoprotein complex subunit, H/ACA ribonucleoprotein complex subunit 2-like protein, H/ACA ribonucleoprotein complex subunit 3, ... (5 entities in total)
Functional Keywordspseudouridine synthase, enzyme complex, snorna, snornp, rna binding protein
Biological sourceTrichoplusia ni (cabbage looper)
More
Total number of polymer chains9
Total formula weight242440.01
Authors
Panwar, H.S.,Worden, E.W. (deposition date: 2025-09-26, release date: 2025-12-10, Last modification date: 2025-12-31)
Primary citationPanwar, H.S.,Vos, T.J.,Xie, X.,Jang, H.J.,Lee, H.,Sheldon, R.D.,Worden, E.J.,Kothe, U.
Interprotomer communication and functional asymmetry in H/ACA snoRNPs.
Proc.Natl.Acad.Sci.USA, 122:e2514683122-e2514683122, 2025
Cited by
PubMed Abstract: H/ACA small nucleolar ribonucleoproteins (H/ACA snoRNPs) facilitate essential cellular processes such as RNA modification, folding, and stability. Here, we present multiple cryo-EM structures of endogenous insect H/ACA snoRNPs containing two protomers assembled on a two-hairpin H/ACA snoRNA. By characterizing key protein-protein and protein-RNA interactions, we reveal the coordination of pseudouridylation activity across the two protomers which explains the predominance of two-hairpin structures in eukaryotic H/ACA snoRNAs. Moreover, we found that several mutations in H/ACA proteins associated with dyskeratosis congenita (DC) directly impair pseudouridine formation suggesting how these mutations disrupt RNA modification and ribosome biogenesis in this disease. Additionally, we uncover coordinated structural changes between Nop10, Nhp2, and the N-terminal extensions of Cbf5 in the 3' protomer that resemble active and inactive conformations and may regulate H/ACA snoRNP activity. In summary, this study provides detailed insight into the structure and function of RNA modification-competent H/ACA snoRNPs, which play pivotal roles in cellular processes including ribosome biogenesis, rRNA folding, (m)RNA modification, and telomere maintenance.
PubMed: 41410763
DOI: 10.1073/pnas.2514683122
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.95 Å)
Structure validation

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