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8OUE

The H/ACA RNP lobe of human telomerase with the dyskerin thumb loop in a semi-closed conformation

This is a non-PDB format compatible entry.
Summary for 8OUE
Entry DOI10.2210/pdb8oue/pdb
Related8OUF
EMDB information17190
DescriptorH/ACA ribonucleoprotein complex subunit DKC1, H/ACA ribonucleoprotein complex subunit 1, H/ACA ribonucleoprotein complex subunit 2, ... (6 entities in total)
Functional Keywordstelomerase, h/aca, pseudouridylation, ribonucleoprotein, rna binding protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains10
Total formula weight415061.33
Authors
Ghanim, G.E.,Sekne, Z.,van Roon, A.M.M.,Balch, S.,Nguyen, T.H.D. (deposition date: 2023-04-22, release date: 2024-01-31, Last modification date: 2024-02-07)
Primary citationGhanim, G.E.,Sekne, Z.,Balch, S.,van Roon, A.M.,Nguyen, T.H.D.
2.7 angstrom cryo-EM structure of human telomerase H/ACA ribonucleoprotein.
Nat Commun, 15:746-746, 2024
Cited by
PubMed Abstract: Telomerase is a ribonucleoprotein (RNP) enzyme that extends telomeric repeats at eukaryotic chromosome ends to counterbalance telomere loss caused by incomplete genome replication. Human telomerase is comprised of two distinct functional lobes tethered by telomerase RNA (hTR): a catalytic core, responsible for DNA extension; and a Hinge and ACA (H/ACA) box RNP, responsible for telomerase biogenesis. H/ACA RNPs also have a general role in pseudouridylation of spliceosomal and ribosomal RNAs, which is critical for the biogenesis of the spliceosome and ribosome. Much of our structural understanding of eukaryotic H/ACA RNPs comes from structures of the human telomerase H/ACA RNP. Here we report a 2.7 Å cryo-electron microscopy structure of the telomerase H/ACA RNP. The significant improvement in resolution over previous 3.3 Å to 8.2 Å structures allows us to uncover new molecular interactions within the H/ACA RNP. Many disease mutations are mapped to these interaction sites. The structure also reveals unprecedented insights into a region critical for pseudouridylation in canonical H/ACA RNPs. Together, our work advances understanding of telomerase-related disease mutations and the mechanism of pseudouridylation by eukaryotic H/ACA RNPs.
PubMed: 38272871
DOI: 10.1038/s41467-024-45002-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.7 Å)
Structure validation

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PDB entries from 2024-11-20

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